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Q13322

- GRB10_HUMAN

UniProt

Q13322 - GRB10_HUMAN

Protein

Growth factor receptor-bound protein 10

Gene

GRB10

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 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. May play a role in mediating insulin-stimulated ubiquitination of INSR, leading to proteasomal degradation. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2.4 Publications

    Enzyme regulationi

    Phosphorylation by mTORC1 stabilizes and activates GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-dependent signaling.1 Publication

    GO - Molecular functioni

    1. insulin receptor binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. insulin-like growth factor receptor signaling pathway Source: Ensembl
    2. insulin receptor signaling pathway Source: BHF-UCL
    3. negative regulation of glucose import Source: BHF-UCL
    4. negative regulation of glycogen biosynthetic process Source: Ensembl
    5. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
    6. negative regulation of phosphorylation Source: Ensembl
    7. negative regulation of Wnt signaling pathway Source: UniProtKB
    8. positive regulation of phosphorylation Source: Ensembl
    9. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    10. response to insulin Source: BHF-UCL

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_508. Signal attenuation.
    SignaLinkiQ13322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth factor receptor-bound protein 10
    Alternative name(s):
    GRB10 adapter protein
    Insulin receptor-binding protein Grb-IR
    Gene namesi
    Name:GRB10
    Synonyms:GRBIR, KIAA0207
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4564. GRB10.

    Subcellular locationi

    Cytoplasm By similarity
    Note: When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes before the sorting of the receptor to the lysosomal compartment By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi104 – 1041S → G: No effect on phosphorylation. 1 Publication
    Mutagenesisi134 – 1341S → A: No effect on YWHAE-binding. 1 Publication
    Mutagenesisi136 – 1361P → A: No effect on NEDD4-binding; when associated with A-139 and A-141. 1 Publication
    Mutagenesisi139 – 1391P → A: No effect on NEDD4-binding; when associated with A-136 and A-141. 1 Publication
    Mutagenesisi141 – 1411P → S: No effect on NEDD4-binding; when associated with A-136 and A-139. 1 Publication
    Mutagenesisi150 – 1501S → I: Loss of phosphorylation. 1 Publication
    Mutagenesisi300 – 3001K → A: 2-fold loss of inositide-binding. 1 Publication
    Mutagenesisi305 – 3051K → A: 5-fold loss of inositide-binding. 1 Publication
    Mutagenesisi308 – 3081K → A: 5-fold loss of inositide-binding. 1 Publication
    Mutagenesisi355 – 3551N → G: 5-fold loss of inositide-binding. 1 Publication
    Mutagenesisi418 – 4181S → A: No net loss of phosphorylation, this may be due to a compensatory phosphorylation of T-422 in vitro. 1 Publication
    Mutagenesisi428 – 4281S → A: Impairs YWHAE-binding. 1 Publication
    Mutagenesisi476 – 4761S → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi520 – 5201R → K: No effect on NEDD4-binding. No effect on the disruption of the interaction between INSR and IRS1 and IRS2. 2 Publications

    Organism-specific databases

    PharmGKBiPA28960.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Growth factor receptor-bound protein 10PRO_0000150346Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphotyrosine; by TEC1 Publication
    Modified residuei104 – 1041Phosphoserine1 Publication
    Modified residuei150 – 1501Phosphoserine; by MTOR, MAPK1 and MAPK32 Publications
    Modified residuei418 – 4181Phosphoserine; by MAPK1 and MAPK3; in vitro3 Publications
    Modified residuei428 – 4281Phosphoserine; by MTOR and PKB/AKT12 Publications
    Modified residuei431 – 4311PhosphoserineBy similarity
    Modified residuei476 – 4761Phosphoserine; by MTOR, MAPK1 and MAPK32 Publications

    Post-translational modificationi

    Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation By similarity. Phosphorylated at Tyr-67 by TEC.By similarity6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13322.
    PaxDbiQ13322.
    PRIDEiQ13322.

    PTM databases

    PhosphoSiteiQ13322.

    Expressioni

    Tissue specificityi

    Widely expressed in fetal and adult tissues, including fetal and postnatal liver, lung, kidney, skeletal muscle, heart, spleen, skin and brain.1 Publication

    Gene expression databases

    ArrayExpressiQ13322.
    BgeeiQ13322.
    CleanExiHS_GRB10.
    GenevestigatoriQ13322.

    Organism-specific databases

    HPAiCAB019423.
    HPA027502.

    Interactioni

    Subunit structurei

    Interacts with ligand-activated tyrosine kinase receptors, including FGFR1, INSR, IGF1R, MET and PDGFRB in a phosphotyrosine-dependent manner through the SH2 domain By similarity. Poorly binds to the EGFR By similarity. Directly interacts with MAP3K14/NIK and is recruited to the EGFR-ERBB2 complex. Interacts with GIGYF1/PERQ1 and GIGYF2/TNRC15 By similarity. When unphosphorylated, interacts with AKT1 and when phosphorylated with YWHAE/14-3-3 epsilon. Interacts with NEDD4. Interacts with LRP6, thus interfering with the binding of AXIN1 to LRP6 By similarity. Binds to activated NRAS.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPHB1P547622EBI-80275,EBI-80252
    INSRP062133EBI-80275,EBI-475899

    Protein-protein interaction databases

    BioGridi109144. 29 interactions.
    DIPiDIP-31657N.
    IntActiQ13322. 11 interactions.
    MINTiMINT-1534184.
    STRINGi9606.ENSP00000381793.

    Structurei

    Secondary structure

    1
    594
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1747
    Beta strandi179 – 1846
    Helixi190 – 1989
    Beta strandi209 – 2157
    Turni216 – 2194
    Beta strandi220 – 2234
    Helixi230 – 2356
    Beta strandi242 – 2476
    Turni249 – 2524
    Helixi253 – 2564
    Helixi258 – 2603
    Beta strandi266 – 2694
    Helixi281 – 2855
    Beta strandi291 – 30010
    Beta strandi307 – 3159
    Beta strandi318 – 3247
    Helixi330 – 3323
    Beta strandi333 – 3375
    Beta strandi342 – 3498
    Helixi351 – 3544
    Beta strandi357 – 36610
    Beta strandi377 – 3837
    Helixi384 – 39916
    Helixi401 – 4077
    Helixi500 – 50910
    Beta strandi516 – 5216
    Beta strandi529 – 5357
    Beta strandi538 – 5469
    Beta strandi555 – 5584
    Beta strandi564 – 5663
    Helixi567 – 5748
    Beta strandi581 – 5833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NRVX-ray1.65A/B487-591[»]
    3HK0X-ray2.60A/B164-415[»]
    ProteinModelPortaliQ13322.
    SMRiQ13322. Positions 167-409, 429-465, 487-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13322.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini166 – 25085Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini290 – 399110PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini493 – 57482SH2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PH domain binds relatively non-specifically to several phosphoinositides, including PI5P, PI(4,5)P2, PI(3,4)P2 and PI(3,4,5)P3, with modest affinities.

    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.
    HOVERGENiHBG000468.
    InParanoidiQ13322.
    OMAiESTMGSE.
    OrthoDBiEOG7SFHW7.
    PhylomeDBiQ13322.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist, many of which involve splicing of 5' non-coding exons.

    Isoform 3 (identifier: Q13322-1) [UniParc]FASTAAdd to Basket

    Also known as: Zeta

    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

    MALAGCPDSF LHHPYYQDKV EQTPRSQQDP AGPGLPAQSD RLANHQEDDV    50
    DLEALVNDMN ASLESLYSAC SMQSDTVPLL QNGQHARSQP RASGPPRSIQ 100
    PQVSPRQRVQ RSQPVHILAV RRLQEEDQQF RTSSLPAIPN PFPELCGPGS 150
    PPVLTPGSLP PSQAAAKQDV KVFSEDGTSK VVEILADMTA RDLCQLLVYK 200
    SHCVDDNSWT LVEHHPHLGL ERCLEDHELV VQVESTMASE SKFLFRKNYA 250
    KYEFFKNPMN FFPEQMVTWC QQSNGSQTQL LQNFLNSSSC PEIQGFLHVK 300
    ELGKKSWKKL YVCLRRSGLY CSTKGTSKEP RHLQLLADLE DSNIFSLIAG 350
    RKQYNAPTDH GLCIKPNKVR NETKELRLLC AEDEQTRTCW MTAFRLLKYG 400
    MLLYQNYRIP QQRKALLSPF STPVRSVSEN SLVAMDFSGQ TGRVIENPAE 450
    AQSAALEEGH AWRKRSTRMN ILGSQSPLHP STLSTVIHRT QHWFHGRISR 500
    EESHRIIKQQ GLVDGLFLLR DSQSNPKAFV LTLCHHQKIK NFQILPCEDD 550
    GQTFFSLDDG NTKFSDLIQL VDFYQLNKGV LPCKLKHHCI RVAL 594
    Length:594
    Mass (Da):67,231
    Last modified:July 15, 1999 - v2
    Checksum:i53A5F885E17C6C6B
    GO
    Isoform 1 (identifier: Q13322-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         283-328: Missing.

    Show »
    Length:548
    Mass (Da):62,026
    Checksum:iFCAA0792DBEB8AC3
    GO
    Isoform 2 (identifier: Q13322-3) [UniParc]FASTAAdd to Basket

    Also known as: Gamma, Beta, SV-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: Missing.

    Show »
    Length:536
    Mass (Da):60,848
    Checksum:i626377A169AE6530
    GO
    Isoform 4 (identifier: Q13322-4) [UniParc]FASTAAdd to Basket

    Also known as: Epsilon

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MALAGCPDSFLHHPYYQ → MQAAGPLFRSK

    Note: No experimental confirmation available.

    Show »
    Length:588
    Mass (Da):66,487
    Checksum:iB5EE8FA86A240D21
    GO

    Sequence cautioni

    The sequence BAA13198.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521P → A in BAA13198. (PubMed:9039502)Curated
    Sequence conflicti400 – 4001G → E in AAB08431. (PubMed:9006901)Curated
    Sequence conflicti428 – 4281S → F in BAF82200. (PubMed:14702039)Curated
    Sequence conflicti498 – 4981I → F in AAB08431. (PubMed:9006901)Curated
    Sequence conflicti541 – 5411N → I in AAC50671. (PubMed:8798417)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361P → L.
    Corresponds to variant rs35647889 [ dbSNP | Ensembl ].
    VAR_053112
    Natural varianti95 – 951P → S.1 Publication
    Corresponds to variant rs80244589 [ dbSNP | Ensembl ].
    VAR_062864
    Natural varianti558 – 5581D → H.
    Corresponds to variant rs11768472 [ dbSNP | Ensembl ].
    VAR_053113

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858Missing in isoform 2. 4 PublicationsVSP_001842Add
    BLAST
    Alternative sequencei1 – 1717MALAG…HPYYQ → MQAAGPLFRSK in isoform 4. 1 PublicationVSP_038784Add
    BLAST
    Alternative sequencei283 – 32846Missing in isoform 1. 2 PublicationsVSP_001843Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34355 mRNA. Translation: AAA88819.1.
    U66065 mRNA. Translation: AAC50671.1.
    U69276 mRNA. Translation: AAB08431.1.
    AF001534 mRNA. Translation: AAB81134.1.
    AF000017 mRNA. Translation: AAC19748.1.
    AB000731 mRNA. Translation: BAF76353.1.
    AJ271366 mRNA. Translation: CAB96542.1.
    D86962 mRNA. Translation: BAA13198.2. Different initiation.
    AK289511 mRNA. Translation: BAF82200.1.
    AF073378
    , AF073363, AF073364, AF073365, AF073366, AF073367, AF073368, AF073369, AF073370, AF073371, AF073372, AF073373, AF073374, AF073375, AF073376, AF073377 Genomic DNA. Translation: AAC83655.1.
    AF073378
    , AF073363, AF073364, AF073365, AF073366, AF073367, AF073368, AF073369, AF073371, AF073372, AF073373, AF073374, AF073375, AF073376, AF073377 Genomic DNA. Translation: AAC83654.1.
    AC005153 Genomic DNA. No translation available.
    CH236955 Genomic DNA. Translation: EAL23897.1.
    CH471128 Genomic DNA. Translation: EAW60964.1.
    CH471128 Genomic DNA. Translation: EAW60965.1.
    CH471128 Genomic DNA. Translation: EAW60967.1.
    BC024285 mRNA. Translation: AAH24285.1.
    CCDSiCCDS43582.1. [Q13322-1]
    CCDS43583.1. [Q13322-3]
    CCDS47586.1. [Q13322-2]
    PIRiI39175.
    RefSeqiNP_001001549.1. NM_001001549.2. [Q13322-2]
    NP_001001550.1. NM_001001550.2. [Q13322-3]
    NP_001001555.1. NM_001001555.2. [Q13322-3]
    NP_005302.3. NM_005311.4. [Q13322-1]
    XP_005271817.1. XM_005271760.1. [Q13322-1]
    XP_005271818.1. XM_005271761.2. [Q13322-1]
    XP_005271822.1. XM_005271765.1. [Q13322-3]
    XP_005271823.1. XM_005271766.2. [Q13322-3]
    XP_006715766.1. XM_006715703.1. [Q13322-1]
    XP_006715767.1. XM_006715704.1. [Q13322-4]
    XP_006715768.1. XM_006715705.1. [Q13322-3]
    UniGeneiHs.164060.

    Genome annotation databases

    EnsembliENST00000335866; ENSP00000338543; ENSG00000106070. [Q13322-3]
    ENST00000357271; ENSP00000349818; ENSG00000106070. [Q13322-2]
    ENST00000398810; ENSP00000381790; ENSG00000106070. [Q13322-3]
    ENST00000398812; ENSP00000381793; ENSG00000106070. [Q13322-1]
    ENST00000401949; ENSP00000385770; ENSG00000106070. [Q13322-1]
    ENST00000402497; ENSP00000385748; ENSG00000106070. [Q13322-3]
    ENST00000402578; ENSP00000385189; ENSG00000106070. [Q13322-3]
    ENST00000403097; ENSP00000385544; ENSG00000106070. [Q13322-4]
    ENST00000406641; ENSP00000385366; ENSG00000106070. [Q13322-3]
    ENST00000407526; ENSP00000385046; ENSG00000106070. [Q13322-3]
    GeneIDi2887.
    KEGGihsa:2887.
    UCSCiuc003tph.3. human. [Q13322-1]
    uc003tpj.2. human. [Q13322-2]
    uc003tpl.2. human. [Q13322-4]

    Polymorphism databases

    DMDMi6166186.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34355 mRNA. Translation: AAA88819.1 .
    U66065 mRNA. Translation: AAC50671.1 .
    U69276 mRNA. Translation: AAB08431.1 .
    AF001534 mRNA. Translation: AAB81134.1 .
    AF000017 mRNA. Translation: AAC19748.1 .
    AB000731 mRNA. Translation: BAF76353.1 .
    AJ271366 mRNA. Translation: CAB96542.1 .
    D86962 mRNA. Translation: BAA13198.2 . Different initiation.
    AK289511 mRNA. Translation: BAF82200.1 .
    AF073378
    , AF073363 , AF073364 , AF073365 , AF073366 , AF073367 , AF073368 , AF073369 , AF073370 , AF073371 , AF073372 , AF073373 , AF073374 , AF073375 , AF073376 , AF073377 Genomic DNA. Translation: AAC83655.1 .
    AF073378
    , AF073363 , AF073364 , AF073365 , AF073366 , AF073367 , AF073368 , AF073369 , AF073371 , AF073372 , AF073373 , AF073374 , AF073375 , AF073376 , AF073377 Genomic DNA. Translation: AAC83654.1 .
    AC005153 Genomic DNA. No translation available.
    CH236955 Genomic DNA. Translation: EAL23897.1 .
    CH471128 Genomic DNA. Translation: EAW60964.1 .
    CH471128 Genomic DNA. Translation: EAW60965.1 .
    CH471128 Genomic DNA. Translation: EAW60967.1 .
    BC024285 mRNA. Translation: AAH24285.1 .
    CCDSi CCDS43582.1. [Q13322-1 ]
    CCDS43583.1. [Q13322-3 ]
    CCDS47586.1. [Q13322-2 ]
    PIRi I39175.
    RefSeqi NP_001001549.1. NM_001001549.2. [Q13322-2 ]
    NP_001001550.1. NM_001001550.2. [Q13322-3 ]
    NP_001001555.1. NM_001001555.2. [Q13322-3 ]
    NP_005302.3. NM_005311.4. [Q13322-1 ]
    XP_005271817.1. XM_005271760.1. [Q13322-1 ]
    XP_005271818.1. XM_005271761.2. [Q13322-1 ]
    XP_005271822.1. XM_005271765.1. [Q13322-3 ]
    XP_005271823.1. XM_005271766.2. [Q13322-3 ]
    XP_006715766.1. XM_006715703.1. [Q13322-1 ]
    XP_006715767.1. XM_006715704.1. [Q13322-4 ]
    XP_006715768.1. XM_006715705.1. [Q13322-3 ]
    UniGenei Hs.164060.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NRV X-ray 1.65 A/B 487-591 [» ]
    3HK0 X-ray 2.60 A/B 164-415 [» ]
    ProteinModelPortali Q13322.
    SMRi Q13322. Positions 167-409, 429-465, 487-593.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109144. 29 interactions.
    DIPi DIP-31657N.
    IntActi Q13322. 11 interactions.
    MINTi MINT-1534184.
    STRINGi 9606.ENSP00000381793.

    PTM databases

    PhosphoSitei Q13322.

    Polymorphism databases

    DMDMi 6166186.

    Proteomic databases

    MaxQBi Q13322.
    PaxDbi Q13322.
    PRIDEi Q13322.

    Protocols and materials databases

    DNASUi 2887.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335866 ; ENSP00000338543 ; ENSG00000106070 . [Q13322-3 ]
    ENST00000357271 ; ENSP00000349818 ; ENSG00000106070 . [Q13322-2 ]
    ENST00000398810 ; ENSP00000381790 ; ENSG00000106070 . [Q13322-3 ]
    ENST00000398812 ; ENSP00000381793 ; ENSG00000106070 . [Q13322-1 ]
    ENST00000401949 ; ENSP00000385770 ; ENSG00000106070 . [Q13322-1 ]
    ENST00000402497 ; ENSP00000385748 ; ENSG00000106070 . [Q13322-3 ]
    ENST00000402578 ; ENSP00000385189 ; ENSG00000106070 . [Q13322-3 ]
    ENST00000403097 ; ENSP00000385544 ; ENSG00000106070 . [Q13322-4 ]
    ENST00000406641 ; ENSP00000385366 ; ENSG00000106070 . [Q13322-3 ]
    ENST00000407526 ; ENSP00000385046 ; ENSG00000106070 . [Q13322-3 ]
    GeneIDi 2887.
    KEGGi hsa:2887.
    UCSCi uc003tph.3. human. [Q13322-1 ]
    uc003tpj.2. human. [Q13322-2 ]
    uc003tpl.2. human. [Q13322-4 ]

    Organism-specific databases

    CTDi 2887.
    GeneCardsi GC07M050625.
    HGNCi HGNC:4564. GRB10.
    HPAi CAB019423.
    HPA027502.
    MIMi 601523. gene.
    neXtProti NX_Q13322.
    PharmGKBi PA28960.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307156.
    HOVERGENi HBG000468.
    InParanoidi Q13322.
    OMAi ESTMGSE.
    OrthoDBi EOG7SFHW7.
    PhylomeDBi Q13322.
    TreeFami TF317511.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_508. Signal attenuation.
    SignaLinki Q13322.

    Miscellaneous databases

    EvolutionaryTracei Q13322.
    GeneWikii GRB10.
    GenomeRNAii 2887.
    NextBioi 11401.
    PROi Q13322.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13322.
    Bgeei Q13322.
    CleanExi HS_GRB10.
    Genevestigatori Q13322.

    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. "Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function."
      Liu F., Roth R.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:10287-10291(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    2. "Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the insulin and insulin-like growth factor I receptors. Evidence for a role in mitogenic signaling."
      O'Neill T.J., Rose D.W., Pillay T.S., Hotta K., Olefsky J.M., Gustafson T.A.
      J. Biol. Chem. 271:22506-22513(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Skeletal muscle.
    3. "Human GRB-IR-beta/GRB10: splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains."
      Frantz J.D., Giorgetti-Peraldi S., Ottinger E.A., Shoelson S.E.
      J. Biol. Chem. 272:2659-2667(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Cerebellum and Skeletal muscle.
    4. "Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma."
      Dong L.Q., Du H., Porter S.G., Kolakowski L.F. Jr., Lee A.V., Mandarino L.J., Fan J., Yee D., Liu F.
      J. Biol. Chem. 272:29104-29112(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases."
      Nantel A., Mohammad-Ali K., Sherk J., Posner B.I., Thomas D.Y.
      J. Biol. Chem. 273:10475-10484(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT TYR-67.
    7. "Genomic structure of the gene for the SH2 and pleckstrin homology domain-containing protein GRB10 and evaluation of its role in Hirschsprung disease."
      Angrist M., Bolk S., Bentley K., Nallasamy S., Halushka M.K., Chakravarti A.
      Oncogene 17:3065-3070(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 3).
    8. "Human GRB10 is imprinted and expressed from the paternal and maternal allele in a highly tissue- and isoform-specific fashion."
      Blagitko N., Mergenthaler S., Schulz U., Wollmann H.A., Craigen W., Eggermann T., Ropers H.-H., Kalscheuer V.M.
      Hum. Mol. Genet. 9:1587-1595(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, IMPRINTING.
      Tissue: Testis.
    9. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Bone marrow.
    10. "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: Cerebellum.
    11. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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 2).
      Tissue: Kidney.
    15. "Phosphorylation of Grb10 by mitogen-activated protein kinase: identification of Ser150 and Ser476 of human Grb10zeta as major phosphorylation sites."
      Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F.
      Biochemistry 44:8890-8897(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 415-425, PHOSPHORYLATION AT SER-150; SER-418 AND SER-476, MUTAGENESIS OF SER-104; SER-150; SER-418 AND SER-476.
    16. "Evidence against GRB10 as the gene responsible for Silver-Russell syndrome."
      McCann J.A., Zheng H., Islam A., Goodyer C.G., Polychronakos C.
      Biochem. Biophys. Res. Commun. 286:943-948(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, IMPRINTING.
    17. "Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the association of IRS-1/IRS-2 with the insulin receptor."
      Wick K.R., Werner E.D., Langlais P., Ramos F.J., Dong L.Q., Shoelson S.E., Liu F.
      J. Biol. Chem. 278:8460-8467(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH INSR, MUTAGENESIS OF ARG-520.
    18. "NIK is a component of the EGF/heregulin receptor signaling complexes."
      Chen D., Xu L.G., Chen L., Li L., Zhai Z., Shu H.B.
      Oncogene 22:4348-4355(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K14, IDENTIFICATION IN A COMPLEX WITH EGFR AND ERBB2.
    19. "Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-2 degradation."
      Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R., Kumar S., Van Obberghen E., Giorgetti-Peraldi S.
      J. Biol. Chem. 279:26754-26761(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEDD4, MUTAGENESIS OF PRO-136; PRO-139; PRO-141 AND ARG-520.
    20. "Phosphorylation of grb10 regulates its interaction with 14-3-3."
      Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.
      J. Biol. Chem. 280:16987-16993(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YWHAE, PHOSPHORYLATION AT SER-428, MUTAGENESIS OF SER-134 AND SER-428.
    21. "Grb10 mediates insulin-stimulated degradation of the insulin receptor: a mechanism of negative regulation."
      Ramos F.J., Langlais P.R., Hu D., Dong L.Q., Liu F.
      Am. J. Physiol. 290:E1262-E1266(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN THE UBIQUITINATION OF INSR.
    22. "GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway."
      Tezuka N., Brown A.M., Yanagawa S.
      Biochem. Biophys. Res. Commun. 356:648-654(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Reciprocal imprinting of human GRB10 in placental trophoblast and brain: evolutionary conservation of reversed allelic expression."
      Monk D., Arnaud P., Frost J., Hills F.A., Stanier P., Feil R., Moore G.E.
      Hum. Mol. Genet. 18:3066-3074(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IMPRINTING.
    26. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling."
      Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D., Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.
      Science 332:1317-1322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-150; SER-428 AND SER-476 BY MTOR, ENZYME REGULATION.
    29. "Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity."
      Stein E.G., Ghirlando R., Hubbard S.R.
      J. Biol. Chem. 278:13257-13264(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 487-591.
    30. "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: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 164-415, INTERACTION WITH NRAS AND PHOSPHOINOSITIDES, MUTAGENESIS OF LYS-300; LYS-305; LYS-308 AND ASN-355.
    31. Erratum
      Depetris R.S., Wu J., Hubbard S.R.
      Nat. Struct. Mol. Biol. 16:1331-1331(2009)
    32. "Imprinting of human GRB10 and its mutations in two patients with Russell-Silver syndrome."
      Yoshihashi H., Maeyama K., Kosaki R., Ogata T., Tsukahara M., Goto Y., Hata J., Matsuo N., Smith R.J., Kosaki K.
      Am. J. Hum. Genet. 67:476-482(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-95, IMPRINTING.

    Entry informationi

    Entry nameiGRB10_HUMAN
    AccessioniPrimary (citable) accession number: Q13322
    Secondary accession number(s): A4D258
    , A7VJ95, A8K0E6, D3DVM9, O00427, O00701, O75222, Q92606, Q92907, Q92948
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 154 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

    Miscellaneous

    The GRB10 locus is imprinted. During embryonic development, the expression in the brain and spinal cord is from the paternal allele, while in placental villous trophoblasts and skeletal muscle, it is from the maternal one. Expression is biallelic in most other tissues. Paternal expression in the brain is maintained throughout adulthood. Imprinting often is isoform-specific.
    GRB10 is unlikely to be responsible for Silver-Russell syndrome (SRS).

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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