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P16333

- NCK1_HUMAN

UniProt

P16333 - NCK1_HUMAN

Protein

Cytoplasmic protein NCK1

Gene

NCK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors.6 Publications

    GO - Molecular functioni

    1. cytoskeletal adaptor activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein kinase inhibitor activity Source: UniProtKB
    4. receptor binding Source: UniProtKB
    5. receptor signaling complex scaffold activity Source: UniProtKB
    6. receptor tyrosine kinase binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. axon guidance Source: Reactome
    3. cell migration Source: Ensembl
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. lamellipodium assembly Source: Ensembl
    7. negative regulation of cell death Source: UniProtKB
    8. negative regulation of protein kinase activity Source: GOC
    9. positive regulation of actin filament polymerization Source: UniProtKB
    10. positive regulation of T cell proliferation Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. regulation of translation Source: UniProtKB-KW
    13. response to other organism Source: Ensembl
    14. signal complex assembly Source: UniProtKB
    15. T cell activation Source: UniProtKB
    16. T cell receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Translation regulation

    Enzyme and pathway databases

    ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12623. Generation of second messenger molecules.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_17025. Downstream signal transduction.
    REACT_19226. Activation of Rac.
    REACT_22351. DCC mediated attractive signaling.
    REACT_23832. Nephrin interactions.
    SignaLinkiP16333.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytoplasmic protein NCK1
    Alternative name(s):
    NCK adaptor protein 1
    Short name:
    Nck-1
    SH2/SH3 adaptor protein NCK-alpha
    Gene namesi
    Name:NCK1
    Synonyms:NCK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7664. NCK1.

    Subcellular locationi

    Cytoplasm. Endoplasmic reticulum. Nucleus
    Note: Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: Reactome
    6. vesicle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-143 and K-229. 1 Publication
    Mutagenesisi143 – 1431W → K: No effect on RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. 1 Publication
    Mutagenesisi229 – 2291W → K: Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229. 1 Publication
    Mutagenesisi308 – 3081R → K: No effect on RASA1-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA31466.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 377376Cytoplasmic protein NCK1PRO_0000096766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei85 – 851Phosphoserine2 Publications
    Modified residuei91 – 911Phosphoserine1 Publication
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei105 – 1051Phosphotyrosine3 Publications

    Post-translational modificationi

    Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16333.
    PaxDbiP16333.
    PeptideAtlasiP16333.
    PRIDEiP16333.

    PTM databases

    PhosphoSiteiP16333.

    Miscellaneous databases

    PMAP-CutDBP16333.

    Expressioni

    Gene expression databases

    ArrayExpressiP16333.
    BgeeiP16333.
    CleanExiHS_NCK1.
    GenevestigatoriP16333.

    Organism-specific databases

    HPAiCAB005063.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain and SH3 domain 2) with EGFR. Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with PKN2. Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with SOCS7. This interaction is required for nuclear import. Part of a complex containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). Interacts with ADAM15. Interacts with FASLG. Directly interacts with RASA1. Interacts with isoform 4 of MINK1. Interacts with FLT1 (tyrosine phosphorylated). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with EPHB1; activates the JUN cascade to regulate cell adhesion. Interacts with EPHA2. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts with the inactive form of EIF2AK2/PKR.19 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCG5Q9H2222EBI-389883,EBI-1761423
    ABL1P005192EBI-389883,EBI-375543
    ABL2P426844EBI-389883,EBI-1102694
    AGERQ151092EBI-389883,EBI-1646426
    AIREO439182EBI-389883,EBI-1753081
    ARHGEF11O150853EBI-389883,EBI-311099
    ASAP1Q9ULH16EBI-389883,EBI-346622
    ASB16Q96NS52EBI-389883,EBI-1751918
    BAZ2AQ9UIF92EBI-389883,EBI-934890
    BRD4O608852EBI-389883,EBI-723869
    BRPF3Q9ULD43EBI-389883,EBI-1753470
    C6P136712EBI-389883,EBI-1753221
    CASTP208102EBI-389883,EBI-1268770
    CD247P209632EBI-389883,EBI-1165705
    CD3EP077666EBI-389883,EBI-1211297
    CDC27P302603EBI-389883,EBI-994813
    CELSR3Q9NYQ72EBI-389883,EBI-308417
    CHAF1AQ131112EBI-389883,EBI-1020839
    CKAP5Q140083EBI-389883,EBI-310585
    CNTNAP1P783572EBI-389883,EBI-1751903
    CYP4F2P783292EBI-389883,EBI-1752413
    DAB2P980822EBI-389883,EBI-1171238
    DAG1Q141182EBI-389883,EBI-1755945
    DLGAP1O144904EBI-389883,EBI-1753207
    DLGAP2Q9P1A64EBI-389883,EBI-1753397
    DLGAP3O958862EBI-389883,EBI-1752541
    DLGAP4Q9Y2H05EBI-389883,EBI-722139
    DLX4Q929883EBI-389883,EBI-1752755
    DNM1Q051932EBI-389883,EBI-713135
    DOCK3Q8IZD93EBI-389883,EBI-1752361
    DUSP15Q9H1R22EBI-389883,EBI-1752795
    ECT2Q9H8V33EBI-389883,EBI-1054039
    ELK3P419703EBI-389883,EBI-1758534
    EPS15P425662EBI-389883,EBI-396684
    F2RL2O002542EBI-389883,EBI-1751853
    FAM110AQ9BQ892EBI-389883,EBI-1752811
    FCGR2BP319942EBI-389883,EBI-724784
    FCGR2CP319952EBI-389883,EBI-1396036
    FLNBO753693EBI-389883,EBI-352089
    FOXH1O755932EBI-389883,EBI-1759806
    FYBO151173EBI-389883,EBI-1753267
    GAB1Q134803EBI-389883,EBI-517684
    GABBR1Q9UBS53EBI-389883,EBI-724156
    GAD1Q992592EBI-389883,EBI-743184
    GHRP109123EBI-389883,EBI-286316
    GLTSCR1Q9NZM43EBI-389883,EBI-1754943
    GNSP155862EBI-389883,EBI-1752200
    GSTZ1O437082EBI-389883,EBI-748043
    HIST1H1EP104122EBI-389883,EBI-358163
    HNRNPRO433902EBI-389883,EBI-713419
    ID4P479283EBI-389883,EBI-1754719
    ISG20L2Q9H9L32EBI-389883,EBI-751335
    JAK2O606742EBI-389883,EBI-518647
    KDRP359683EBI-389883,EBI-1005487
    KITP107213EBI-389883,EBI-1379503
    KMT2BQ9UMN62EBI-389883,EBI-765774
    LCP2Q1309414EBI-389883,EBI-346946
    LRRC3Q9BY712EBI-389883,EBI-1761329
    MAP4P278162EBI-389883,EBI-715255
    MAP4K1Q929184EBI-389883,EBI-881
    MAP4K5Q9Y4K42EBI-389883,EBI-1279
    MEPEQ9NQ763EBI-389883,EBI-1753293
    METP085812EBI-389883,EBI-1039152
    MYLKQ157462EBI-389883,EBI-968482
    NELFBQ8WX926EBI-389883,EBI-347721
    NKX2-1P436992EBI-389883,EBI-1391923
    NPHS1O605003EBI-389883,EBI-996920
    PAK2Q131772EBI-389883,EBI-1045887
    PDIA2Q130873EBI-389883,EBI-1752525
    PHACTR2O751672EBI-389883,EBI-1754409
    PIK3C2BO007503EBI-389883,EBI-641107
    PNMA2Q9UL422EBI-389883,EBI-302355
    PRXQ9BXM02EBI-389883,EBI-1753064
    PTPN4P290743EBI-389883,EBI-710431
    RAG1P159182EBI-389883,EBI-1755109
    RAPGEF1Q139052EBI-389883,EBI-976876
    RASA1P209366EBI-389883,EBI-1026476
    RIMS2Q9UQ262EBI-389883,EBI-1756749
    RIN3Q8TB242EBI-389883,EBI-1570523
    RPL13P263732EBI-389883,EBI-356849
    RPP38P783452EBI-389883,EBI-366493
    RRASP103013EBI-389883,EBI-968703
    SCARF2Q96GP62EBI-389883,EBI-1752088
    SEMA7AO753262EBI-389883,EBI-1753538
    SEPN1Q9NZV52EBI-389883,EBI-1751965
    SHANK2Q9UPX86EBI-389883,EBI-1570571
    SHANK3Q9BYB04EBI-389883,EBI-1752330
    SHROOM2Q137962EBI-389883,EBI-1644065
    SLC23A1Q9UHI72EBI-389883,EBI-1759386
    SLC24A1O607213EBI-389883,EBI-1753504
    SNX12Q9UMY43EBI-389883,EBI-1752602
    SNX17Q150363EBI-389883,EBI-1752620
    SNX8Q9Y5X22EBI-389883,EBI-1752557
    SOS1Q078895EBI-389883,EBI-297487
    SOS2Q078903EBI-389883,EBI-298181
    SP1P080472EBI-389883,EBI-298336
    SPENQ96T583EBI-389883,EBI-765739
    SUV39H2Q9H5I12EBI-389883,EBI-723127
    SYNJ2O150563EBI-389883,EBI-310513
    TGOLN2O434933EBI-389883,EBI-1752146
    TMPOP421672EBI-389883,EBI-455283
    TPSAB1Q156612EBI-389883,EBI-1761369
    TPX2Q9ULW04EBI-389883,EBI-1037322
    TRAIPQ9BWF23EBI-389883,EBI-1756205
    TRIM39Q9HCM92EBI-389883,EBI-739510
    TULP1O002942EBI-389883,EBI-1756778
    VPS13AQ96RL73EBI-389883,EBI-1752583
    WIPF1O435162EBI-389883,EBI-346356

    Protein-protein interaction databases

    BioGridi110770. 68 interactions.
    DIPiDIP-639N.
    IntActiP16333. 194 interactions.
    MINTiMINT-92747.
    STRINGi9606.ENSP00000288986.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi28 – 336
    Beta strandi35 – 428
    Beta strandi48 – 514
    Turni53 – 553
    Beta strandi56 – 583
    Beta strandi99 – 1013
    Beta strandi109 – 1157
    Beta strandi131 – 1388
    Beta strandi142 – 1487
    Beta strandi151 – 1566
    Helixi157 – 1593
    Beta strandi160 – 1623
    Beta strandi168 – 1703
    Helixi289 – 29911
    Beta strandi304 – 3096
    Beta strandi311 – 3133
    Beta strandi316 – 3216
    Beta strandi324 – 3263
    Beta strandi328 – 3358
    Beta strandi338 – 3414
    Beta strandi344 – 3485
    Helixi349 – 35810
    Beta strandi361 – 3633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CI8X-ray1.80A281-377[»]
    2CI9X-ray1.50A/B281-377[»]
    2CUBNMR-A99-173[»]
    2JS0NMR-A107-165[»]
    2JS2NMR-A1-61[»]
    2JW4NMR-A1-63[»]
    ProteinModelPortaliP16333.
    SMRiP16333. Positions 1-61, 99-174, 193-250, 279-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16333.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 6160SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 16551SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini190 – 25263SH3 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini282 – 37695SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Only the first and third SH3 domains seem to be involved in RASA1-binding; the second SH3 domain and the SH2 domains do not seeem to be involved.

    Sequence similaritiesi

    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 3 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG261435.
    HOGENOMiHOG000290684.
    HOVERGENiHBG000719.
    InParanoidiP16333.
    KOiK07365.
    OMAiTIMQNNP.
    OrthoDBiEOG7SV0VJ.
    PhylomeDBiP16333.
    TreeFamiTF351631.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR017304. NCK.
    IPR028526. NCK1.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR22820:SF11. PTHR22820:SF11. 1 hit.
    PfamiPF00017. SH2. 1 hit.
    PF00018. SH3_1. 2 hits.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037874. Cytoplasmic_NCK. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 3 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 3 hits.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    PS50002. SH3. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P16333-1) [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

    MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF    50
    VPSNYVERKN SARKASIVKN LKDTLGIGKV KRKPSVPDSA SPADDSFVDP 100
    GERLYDLNMP AYVKFNYMAE REDELSLIKG TKVIVMEKCS DGWWRGSYNG 150
    QVGWFPSNYV TEEGDSPLGD HVGSLSEKLA AVVNNLNTGQ VLHVVQALYP 200
    FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG LVPKNYVTVM 250
    QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG 300
    HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME 350
    ELVEHYKKAP IFTSEQGEKL YLVKHLS 377
    Length:377
    Mass (Da):42,864
    Last modified:August 1, 1990 - v1
    Checksum:i554E9B1A936AEF30
    GO
    Isoform 2 (identifier: P16333-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: MAEEVVVVAK...IVKNLKDTLG → MDWLNVFKDFFS

    Note: No experimental confirmation available.

    Show »
    Length:313
    Mass (Da):35,511
    Checksum:iD10F0F2DEF1D72F7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti180 – 1801A → V.
    Corresponds to variant rs13320485 [ dbSNP | Ensembl ].
    VAR_051228

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7676MAEEV…KDTLG → MDWLNVFKDFFS in isoform 2. 1 PublicationVSP_043122Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17576 mRNA. Translation: CAA35599.1.
    AK301460 mRNA. Translation: BAH13487.1.
    AC011597 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79105.1.
    CH471052 Genomic DNA. Translation: EAW79108.1.
    CH471052 Genomic DNA. Translation: EAW79109.1.
    BC006403 mRNA. Translation: AAH06403.1.
    CCDSiCCDS3092.1. [P16333-1]
    CCDS54644.1. [P16333-2]
    PIRiS08636.
    RefSeqiNP_001177725.1. NM_001190796.2. [P16333-2]
    NP_006144.1. NM_006153.5. [P16333-1]
    XP_006713713.1. XM_006713650.1. [P16333-1]
    XP_006713714.1. XM_006713651.1. [P16333-1]
    XP_006713715.1. XM_006713652.1. [P16333-1]
    UniGeneiHs.126889.
    Hs.477693.

    Genome annotation databases

    EnsembliENST00000288986; ENSP00000288986; ENSG00000158092. [P16333-1]
    ENST00000469404; ENSP00000419631; ENSG00000158092. [P16333-2]
    ENST00000481752; ENSP00000417273; ENSG00000158092. [P16333-1]
    GeneIDi4690.
    KEGGihsa:4690.
    UCSCiuc003erh.3. human. [P16333-1]
    uc011bme.2. human. [P16333-2]

    Polymorphism databases

    DMDMi127962.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17576 mRNA. Translation: CAA35599.1 .
    AK301460 mRNA. Translation: BAH13487.1 .
    AC011597 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79105.1 .
    CH471052 Genomic DNA. Translation: EAW79108.1 .
    CH471052 Genomic DNA. Translation: EAW79109.1 .
    BC006403 mRNA. Translation: AAH06403.1 .
    CCDSi CCDS3092.1. [P16333-1 ]
    CCDS54644.1. [P16333-2 ]
    PIRi S08636.
    RefSeqi NP_001177725.1. NM_001190796.2. [P16333-2 ]
    NP_006144.1. NM_006153.5. [P16333-1 ]
    XP_006713713.1. XM_006713650.1. [P16333-1 ]
    XP_006713714.1. XM_006713651.1. [P16333-1 ]
    XP_006713715.1. XM_006713652.1. [P16333-1 ]
    UniGenei Hs.126889.
    Hs.477693.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CI8 X-ray 1.80 A 281-377 [» ]
    2CI9 X-ray 1.50 A/B 281-377 [» ]
    2CUB NMR - A 99-173 [» ]
    2JS0 NMR - A 107-165 [» ]
    2JS2 NMR - A 1-61 [» ]
    2JW4 NMR - A 1-63 [» ]
    ProteinModelPortali P16333.
    SMRi P16333. Positions 1-61, 99-174, 193-250, 279-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110770. 68 interactions.
    DIPi DIP-639N.
    IntActi P16333. 194 interactions.
    MINTi MINT-92747.
    STRINGi 9606.ENSP00000288986.

    Chemistry

    BindingDBi P16333.
    ChEMBLi CHEMBL4846.

    PTM databases

    PhosphoSitei P16333.

    Polymorphism databases

    DMDMi 127962.

    Proteomic databases

    MaxQBi P16333.
    PaxDbi P16333.
    PeptideAtlasi P16333.
    PRIDEi P16333.

    Protocols and materials databases

    DNASUi 4690.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288986 ; ENSP00000288986 ; ENSG00000158092 . [P16333-1 ]
    ENST00000469404 ; ENSP00000419631 ; ENSG00000158092 . [P16333-2 ]
    ENST00000481752 ; ENSP00000417273 ; ENSG00000158092 . [P16333-1 ]
    GeneIDi 4690.
    KEGGi hsa:4690.
    UCSCi uc003erh.3. human. [P16333-1 ]
    uc011bme.2. human. [P16333-2 ]

    Organism-specific databases

    CTDi 4690.
    GeneCardsi GC03P136581.
    HGNCi HGNC:7664. NCK1.
    HPAi CAB005063.
    MIMi 600508. gene.
    neXtProti NX_P16333.
    PharmGKBi PA31466.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261435.
    HOGENOMi HOG000290684.
    HOVERGENi HBG000719.
    InParanoidi P16333.
    KOi K07365.
    OMAi TIMQNNP.
    OrthoDBi EOG7SV0VJ.
    PhylomeDBi P16333.
    TreeFami TF351631.

    Enzyme and pathway databases

    Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12623. Generation of second messenger molecules.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_17025. Downstream signal transduction.
    REACT_19226. Activation of Rac.
    REACT_22351. DCC mediated attractive signaling.
    REACT_23832. Nephrin interactions.
    SignaLinki P16333.

    Miscellaneous databases

    EvolutionaryTracei P16333.
    GeneWikii NCK1.
    GenomeRNAii 4690.
    NextBioi 18086.
    PMAP-CutDB P16333.
    PROi P16333.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16333.
    Bgeei P16333.
    CleanExi HS_NCK1.
    Genevestigatori P16333.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR017304. NCK.
    IPR028526. NCK1.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR22820:SF11. PTHR22820:SF11. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF00018. SH3_1. 2 hits.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037874. Cytoplasmic_NCK. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 3 hits.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    PS50002. SH3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3."
      Lehmann J.M., Riethmueller G., Johnson J.P.
      Nucleic Acids Res. 18:1048-1048(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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 2).
      Tissue: Synovium.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Uterus.
    6. "Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP."
      Park D., Rhee S.G.
      Mol. Cell. Biol. 12:5816-5823(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, PARTIAL PROTEIN SEQUENCE.
    7. "The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment."
      Meisenhelder J., Hunter T.
      Mol. Cell. Biol. 12:5843-5856(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    8. "Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
      Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
      Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION.
    9. "A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs."
      Matuoka K., Miki H., Takahashi K., Takenawa T.
      Biochem. Biophys. Res. Commun. 239:488-492(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOCS7.
    10. "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
      Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
      Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT1.
    11. "BLNK: a central linker protein in B cell activation."
      Fu C., Turck C.W., Kurosaki T., Chan A.C.
      Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK; GRB2; PLCG1 AND VAV.
    12. "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase."
      Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.
      J. Biol. Chem. 273:1303-1308(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH EPHB1.
      Tissue: Kidney.
    13. "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
      Braverman L.E., Quilliam L.A.
      J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EGFR; PAK1; PKN2 AND SOS1, PHOSPHORYLATION.
    14. "Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
      Rebhun J.F., Chen H., Quilliam L.A.
      J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RALGPS1.
    15. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
      Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
      J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV2.
    16. "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
      Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
      Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV2.
    17. "Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta."
      Hu Y., Leo C., Yu S., Huang B.C., Wang H., Shen M., Luo Y., Daniel-Issakani S., Payan D.G., Xu X.
      J. Biol. Chem. 279:54387-54397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MINK1.
    18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
      Latreille M., Larose L.
      J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH PP1 AND PPP1R15B, FUNCTION, SUBCELLULAR LOCATION.
    20. "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
      Lamalice L., Houle F., Huot J.
      J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDR.
    21. "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
      Kremer B.E., Adang L.A., Macara I.G.
      Cell 130:837-850(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOCS7.
    22. "Nck-1 interacts with PKR and modulates its activation by dsRNA."
      Cardin E., Larose L.
      Biochem. Biophys. Res. Commun. 377:231-235(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    24. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
      Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
      Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADAM15.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-91 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    28. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity."
      Ger M., Zitkus Z., Valius M.
      Cell. Signal. 23:1651-1658(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASA1, MUTAGENESIS OF TRP-38; TRP-143; TRP-229 AND ARG-308.
    31. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
      Lee H., Bennett A.M.
      Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH EPHA2.
    34. "Solution structure of the SH3 domain of the human cytoplasmic protein NCK1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 99-174.
    35. "Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor."
      Hake M.J., Choowongkomon K., Kostenko O., Carlin C.R., Sonnichsen F.D.
      Biochemistry 47:3096-3108(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-61 AND 107-165, INTERACTION WITH EGFR.

    Entry informationi

    Entry nameiNCK1_HUMAN
    AccessioniPrimary (citable) accession number: P16333
    Secondary accession number(s): B7Z751, D3DNE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 164 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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