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Q14449

- GRB14_HUMAN

UniProt

Q14449 - GRB14_HUMAN

Protein

Growth factor receptor-bound protein 14

Gene

GRB14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal.2 Publications

    GO - Molecular functioni

    1. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. leukocyte migration Source: Reactome
    3. positive regulation of signal transduction Source: GOC
    4. signal transduction Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_12621. Tie2 Signaling.
    SignaLinkiQ14449.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth factor receptor-bound protein 14
    Alternative name(s):
    GRB14 adapter protein
    Gene namesi
    Name:GRB14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4565. GRB14.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein
    Note: Upon insulin stimulation, translocates to the plasma membrane.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. endosome membrane Source: UniProtKB-SubCell
    4. Golgi membrane Source: UniProtKB-SubCell
    5. intracellular membrane-bounded organelle Source: BHF-UCL
    6. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi140 – 1401K → A: Partial loss of INSR-binding. Loss of inhibition of AKT1 activation. Loss of inhibition of MAPK3 phosphorylation. Loss of NRAS-binding. 1 Publication
    Mutagenesisi245 – 2451E → G: 4-fold increase in PI(3,4,5)P3-binding affinity; when associated with S-246. 1 Publication
    Mutagenesisi246 – 2461Q → S: 4-fold increase in PI(3,4,5)P3-binding affinity; when associated with G-245. 1 Publication
    Mutagenesisi252 – 2521K → A: Partial loss of INSR-binding. Loss of inhibition of AKT1 activation. Loss of inhibition of MAPK3 phosphorylation. Loss of translocation to the plasma membrane upon insulin-stimulation. More than 3-fold decrease in PI(3,4,5)P3-binding affinity. 1 Publication
    Mutagenesisi299 – 2991G → N: No effect on PI(3,4,5)P3-binding. 1 Publication
    Mutagenesisi348 – 3481Q → A: Loss of inhibition of AKT1 activation; when associated with A-349. Loss of inhibition of MAPK3 phosphorylation; when associated with A-349. No effect on INSR-binding; when associated with A-349. 1 Publication
    Mutagenesisi349 – 3491N → A: Loss of inhibition of AKT1 activation; when associated with A-348. Loss of inhibition of MAPK3 phosphorylation; when associated with A-348. No effect on INSR-binding; when associated with A-348. 1 Publication

    Organism-specific databases

    PharmGKBiPA28961.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 540539Growth factor receptor-bound protein 14PRO_0000150348Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Post-translational modificationi

    Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14449.
    PaxDbiQ14449.
    PRIDEiQ14449.

    PTM databases

    PhosphoSiteiQ14449.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the liver, kidney, pancreas, testis, ovary, heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ14449.
    BgeeiQ14449.
    CleanExiHS_GRB14.
    GenevestigatoriQ14449.

    Organism-specific databases

    HPAiCAB022294.
    HPA035052.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor (INSR), through the SH2 domain By similarity. Interacts with GRB14 (via BPS domain); this interaction protects the tyrosines in the activation loop on INSR from dephosphorylation. Binds to the ankyrin repeat region of TNKS2 via its N-terminus. Interacts with activated NRAS. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated).By similarity5 Publications

    Protein-protein interaction databases

    BioGridi109145. 10 interactions.
    DIPiDIP-42605N.
    IntActiQ14449. 5 interactions.
    MINTiMINT-1894128.
    STRINGi9606.ENSP00000263915.

    Structurei

    Secondary structure

    1
    540
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi107 – 1137
    Beta strandi119 – 1257
    Helixi130 – 14112
    Beta strandi149 – 1557
    Turni156 – 1594
    Beta strandi160 – 1634
    Helixi170 – 1756
    Beta strandi184 – 1896
    Helixi195 – 1984
    Turni201 – 2033
    Turni206 – 2083
    Helixi221 – 2299
    Beta strandi236 – 2449
    Beta strandi251 – 2599
    Beta strandi262 – 2687
    Turni274 – 2763
    Beta strandi277 – 2815
    Beta strandi283 – 2919
    Turni297 – 2993
    Beta strandi301 – 3033
    Beta strandi305 – 3106
    Beta strandi312 – 3154
    Beta strandi320 – 3234
    Helixi327 – 34216
    Helixi344 – 3518
    Beta strandi377 – 3804
    Beta strandi382 – 3854
    Helixi392 – 40716
    Helixi434 – 4363
    Helixi446 – 4549
    Turni455 – 4573
    Beta strandi462 – 4676
    Beta strandi469 – 4724
    Beta strandi475 – 4817
    Beta strandi484 – 49512
    Beta strandi498 – 5047
    Beta strandi510 – 5123
    Helixi513 – 5208
    Beta strandi527 – 5293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AUGX-ray2.30A/B433-537[»]
    2AUHX-ray3.20B361-419[»]
    4K81X-ray2.40A/C/E/G106-356[»]
    DisProtiDP00230.
    ProteinModelPortaliQ14449.
    SMRiQ14449. Positions 106-356, 373-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14449.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini106 – 19287Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini234 – 342109PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini439 – 53597SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain binds relatively non-specifically and with low affinity to several phosphoinositides, the best binder being PI(3,4,5)P3.1 Publication

    Sequence similaritiesi

    Belongs to the GRB7/10/14 family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG307156.
    HOGENOMiHOG000231904.
    HOVERGENiHBG000468.
    InParanoidiQ14449.
    OMAiKLKHYCA.
    OrthoDBiEOG7SFHW7.
    PhylomeDBiQ14449.
    TreeFamiTF317511.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR015042. BPS-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR000980. SH2.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF08947. BPS. 1 hit.
    PF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    SMARTiSM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50001. SH2. 1 hit.
    [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: Q14449-1) [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

    MTTSLQDGQS AASRAAARDS PLAAQVCGAA QGRGDAHDLA PAPWLHARAL    50
    LPLPDGTRGC AADRRKKKDL DVPEMPSIPN PFPELCCSPF TSVLSADLFP 100
    KANSRKKQVI KVYSEDETSR ALDVPSDITA RDVCQLLILK NHYIDDHSWT 150
    LFEHLPHIGV ERTIEDHELV IEVLSNWGIE EENKLYFRKN YAKYEFFKNP 200
    MYFFPEHMVS FATETNGEIS PTQILQMFLS SSTYPEIHGF LHAKEQGKKS 250
    WKKIYFFLRR SGLYFSTKGT SKEPRHLQFF SEFGNSDIYV SLAGKKKHGA 300
    PTNYGFCFKP NKAGGPRDLK MLCAEEEQSR TCWVTAIRLL KYGMQLYQNY 350
    MHPYQGRSGC SSQSISPMRS ISENSLVAMD FSGQKSRVIE NPTEALSVAV 400
    EEGLAWRKKG CLRLGTHGSP TASSQSSATN MAIHRSQPWF HHKISRDEAQ 450
    RLIIQQGLVD GVFLVRDSQS NPKTFVLSMS HGQKIKHFQI IPVEDDGEMF 500
    HTLDDGHTRF TDLIQLVEFY QLNKGVLPCK LKHYCARIAL 540
    Length:540
    Mass (Da):60,988
    Last modified:February 15, 2005 - v2
    Checksum:i00472988650F7C6C
    GO
    Isoform 2 (identifier: Q14449-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MTTSLQDGQSAASRAAARDSP → MSLSARRVTLPAITPIILQKR
         22-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:453
    Mass (Da):51,946
    Checksum:i82469B04B7231E1C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901F → I.2 Publications
    Corresponds to variant rs61748245 [ dbSNP | Ensembl ].
    VAR_065758
    Natural varianti507 – 5071H → Y in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065759

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121MTTSL…ARDSP → MSLSARRVTLPAITPIILQK R in isoform 2. 1 PublicationVSP_056582Add
    BLAST
    Alternative sequencei22 – 10887Missing in isoform 2. 1 PublicationVSP_056583Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76687 mRNA. Translation: AAC15861.1.
    AK301961 mRNA. Translation: BAH13595.1.
    AC107075 Genomic DNA. No translation available.
    AC110086 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11342.1.
    BC053559 mRNA. Translation: AAH53559.1.
    CCDSiCCDS2222.1.
    RefSeqiNP_004481.2. NM_004490.2.
    XP_005246534.1. XM_005246477.2.
    UniGeneiHs.411881.

    Genome annotation databases

    EnsembliENST00000263915; ENSP00000263915; ENSG00000115290.
    ENST00000543549; ENSP00000443699; ENSG00000115290.
    GeneIDi2888.
    KEGGihsa:2888.
    UCSCiuc002ucl.3. human.

    Polymorphism databases

    DMDMi59802920.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76687 mRNA. Translation: AAC15861.1 .
    AK301961 mRNA. Translation: BAH13595.1 .
    AC107075 Genomic DNA. No translation available.
    AC110086 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11342.1 .
    BC053559 mRNA. Translation: AAH53559.1 .
    CCDSi CCDS2222.1.
    RefSeqi NP_004481.2. NM_004490.2.
    XP_005246534.1. XM_005246477.2.
    UniGenei Hs.411881.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AUG X-ray 2.30 A/B 433-537 [» ]
    2AUH X-ray 3.20 B 361-419 [» ]
    4K81 X-ray 2.40 A/C/E/G 106-356 [» ]
    DisProti DP00230.
    ProteinModelPortali Q14449.
    SMRi Q14449. Positions 106-356, 373-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109145. 10 interactions.
    DIPi DIP-42605N.
    IntActi Q14449. 5 interactions.
    MINTi MINT-1894128.
    STRINGi 9606.ENSP00000263915.

    PTM databases

    PhosphoSitei Q14449.

    Polymorphism databases

    DMDMi 59802920.

    Proteomic databases

    MaxQBi Q14449.
    PaxDbi Q14449.
    PRIDEi Q14449.

    Protocols and materials databases

    DNASUi 2888.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263915 ; ENSP00000263915 ; ENSG00000115290 .
    ENST00000543549 ; ENSP00000443699 ; ENSG00000115290 .
    GeneIDi 2888.
    KEGGi hsa:2888.
    UCSCi uc002ucl.3. human.

    Organism-specific databases

    CTDi 2888.
    GeneCardsi GC02M165313.
    HGNCi HGNC:4565. GRB14.
    HPAi CAB022294.
    HPA035052.
    MIMi 601524. gene.
    neXtProti NX_Q14449.
    PharmGKBi PA28961.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307156.
    HOGENOMi HOG000231904.
    HOVERGENi HBG000468.
    InParanoidi Q14449.
    OMAi KLKHYCA.
    OrthoDBi EOG7SFHW7.
    PhylomeDBi Q14449.
    TreeFami TF317511.

    Enzyme and pathway databases

    Reactomei REACT_12621. Tie2 Signaling.
    SignaLinki Q14449.

    Miscellaneous databases

    EvolutionaryTracei Q14449.
    GeneWikii GRB14.
    GenomeRNAii 2888.
    NextBioi 11411.
    PROi Q14449.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14449.
    Bgeei Q14449.
    CleanExi HS_GRB14.
    Genevestigatori Q14449.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR015042. BPS-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR000159. Ras-assoc.
    IPR000980. SH2.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF08947. BPS. 1 hit.
    PF00169. PH. 1 hit.
    PF00788. RA. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    SMARTi SM00233. PH. 1 hit.
    SM00314. RA. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50200. RA. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of GRB14, a novel member of the GRB7 gene family."
      Daly R.J., Sanderson G.M., Janes P.W., Sutherland R.L.
      J. Biol. Chem. 271:12502-12510(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-90.
    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: Testis.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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: Skin.
    6. "Inhibition of insulin receptor catalytic activity by the molecular adapter Grb14."
      Bereziat V., Kasus-Jacobi A., Perdereau D., Cariou B., Girard J., Burnol A.F.
      J. Biol. Chem. 277:4845-4852(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSR.
    7. "The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1."
      King C.C., Newton A.C.
      J. Biol. Chem. 279:37518-37527(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDPK1.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14."
      Depetris R.S., Wu J., Hubbard S.R.
      Nat. Struct. Mol. Biol. 16:833-839(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NRAS, PHOSPHOINOSITIDE-BINDING, SUBCELLULAR LOCATION, DOMAIN PH, MUTAGENESIS OF LYS-140; GLU-245; GLN-246; LYS-252; GLY-299; GLN-348 AND ASN-349.
    10. Erratum
      Depetris R.S., Wu J., Hubbard S.R.
      Nat. Struct. Mol. Biol. 16:1331-1331(2009)
    11. "Tyrosine phosphorylation of Grb14 by Tie2."
      Sturk C., Dumont D.J.
      Cell Commun. Signal. 8:30-30(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TEK/TIE2, PHOSPHORYLATION.
    12. "Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14."
      Depetris R.S., Hu J., Gimpelevich I., Holt L.J., Daly R.J., Hubbard S.R.
      Mol. Cell 20:325-333(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 361-419 AND 433-537 IN COMPLEX WITH INSR.
    13. "Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
      Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
      Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-90 AND TYR-507.

    Entry informationi

    Entry nameiGRB14_HUMAN
    AccessioniPrimary (citable) accession number: Q14449
    Secondary accession number(s): B7Z7F9, Q7Z6I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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 2
      Human chromosome 2: 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