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Q60760

- GRB10_MOUSE

UniProt

Q60760 - GRB10_MOUSE

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Protein

Growth factor receptor-bound protein 10

Gene

Grb10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. A similar role in the mediation of ubiquitination has also been suggested with INSR. 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-2.5 Publications

Enzyme regulationi

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

GO - Molecular functioni

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

GO - Biological processi

  1. insulin-like growth factor receptor signaling pathway Source: MGI
  2. insulin receptor signaling pathway Source: Ensembl
  3. negative regulation of glucose import Source: BHF-UCL
  4. negative regulation of glycogen biosynthetic process Source: BHF-UCL
  5. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  6. negative regulation of phosphorylation Source: BHF-UCL
  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. signal transduction Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_188578. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Growth factor receptor-bound protein 10
Alternative name(s):
GRB10 adapter protein
Maternally expressed gene 1 protein
Gene namesi
Name:Grb10
Synonyms:Meg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:103232. Grb10.

Subcellular locationi

Cytoplasm 1 Publication
Note: When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R before the sorting of the receptor to the lysosomal compartment.

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Disruption of the maternal allele results in overgrowth of both the embryo and placenta such that mutant mice are at birth about 30% larger than normal. This effect occurs during embryogenesis and results in addition in disproportionate overgrowth of the liver with relative sparing of the brain. The major part of the growth phenotype seems to be IGF2-independent.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621Growth factor receptor-bound protein 10PRO_0000150347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei96 – 961Phosphoserine; alternate1 Publication
Modified residuei96 – 961Phosphoserine; by MTOR, MAPK1 and MAPK3; alternateBy similarity
Modified residuei455 – 4551Phosphoserine; by MTOR and PKB/AKT1By similarity
Modified residuei458 – 4581Phosphoserine1 Publication
Modified residuei503 – 5031Phosphoserine; by MTOR, MAPK1 and MAPK3By similarity

Post-translational modificationi

Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ60760.
PaxDbiQ60760.
PRIDEiQ60760.

PTM databases

PhosphoSiteiQ60760.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Developmental stagei

At 13.5 dpc, expressed in most embryonic tissues and in placenta. At 14.5 dpc, expressed at high levels in a variety of muscle tissues, including that of the face and trunk, the intercostal muscles, the diaphragm and cardiac muscle, the tongue and limbs (at protein level). In the brain, most abundant expression in the subependymal layers, in the meninges and in the choroid plexus (both epithelium and mesenchyme) (at protein level). High levels in the liver, bronchioles and the cartilage of the atlas, ribs and long bones (at protein level). In the kidney, expression limited to the developing tubules and mesenchyme (at protein level). Also detected in the adrenal gland and pancreatic bud (at protein level). At 12.5 dpc, paternal allele expression detected in the cartilage of the limbs, ribs and face and in the meninges. At 14.5 dpc, paternal allele expressed in the cartilage of the axis, ribs, head, and long bones, in the heart, lungs, gut, umbilicus and tongue, as well as in the meninges of the fourth ventricle. Not detected in the skeletal muscle. In most tissues, paternal expression is lower than maternal.2 Publications

Gene expression databases

BgeeiQ60760.
CleanExiMM_GRB10.
ExpressionAtlasiQ60760. baseline and differential.
GenevestigatoriQ60760.

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. Poorly binds to the EGFR. Directly interacts with MAP3K14/NIK and is recruited to the EGFR-ERBB2 complex (By similarity). Interacts with GIGYF1/PERQ1 and GIGYF2/TNRC15. 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. Binds to activated NRAS (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
InsrP152086EBI-861810,EBI-6999015
Nedd4P469356EBI-861810,EBI-773516

Protein-protein interaction databases

BioGridi200045. 6 interactions.
DIPiDIP-446N.
IntActiQ60760. 8 interactions.
MINTiMINT-102080.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi515 – 5173
Helixi527 – 53610
Beta strandi543 – 5486
Beta strandi556 – 5627
Beta strandi565 – 57612
Beta strandi579 – 5857
Beta strandi588 – 5936
Helixi594 – 6018
Beta strandi608 – 6103

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M7FX-ray2.00A514-621[»]
ProteinModelPortaliQ60760.
SMRiQ60760. Positions 195-437, 456-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 27885Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini318 – 427110PHPROSITE-ProRule annotationAdd
BLAST
Domaini520 – 60182SH2PROSITE-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.By similarity

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.
GeneTreeiENSGT00550000074537.
HOVERGENiHBG000468.
InParanoidiQ60760.
OMAiESTMGSE.
OrthoDBiEOG7SFHW7.
PhylomeDBiQ60760.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q60760-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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

        10         20         30         40         50
MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS
60 70 80 90 100
PRQKMQRSQP VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV
110 120 130 140 150
APSSLPPPPS QPPAKHCGRC EKWIPGENTR GNGKRKIWRW QFPPGFQLSK
160 170 180 190 200
LTRPGLWTKT TARFSKKQPK NQCPTDTVNP VARMPTSQME KLRLRKDVKV
210 220 230 240 250
FSEDGTSKVV EILTDMTARD LCQLLVYKSH CVDDNSWTLV EHHPQLGLER
260 270 280 290 300
CLEDHEIVVQ VESTMPSESK FLFRKNYAKY EFFKNPVNFF PDQMVNWCQQ
310 320 330 340 350
SNGGQAQLLQ NFLNTSSCPE IQGFLQVKEV GRKSWKKLYV CLRRSGLYYS
360 370 380 390 400
TKGTSKEPRH LQLLADLEES SIFYLIAGKK QYNAPNEHGM CIKPNKAKTE
410 420 430 440 450
MKELRLLCAE DEQIRTCWMT AFRLLKYGML LYQNYRIPQR KGLPPPFNAP
460 470 480 490 500
MRSVSENSLV AMDFSGQIGR VIDNPAEAQS AALEEGHAWR KRSTRMNILS
510 520 530 540 550
SQSPLHPSTL NAVIHRTQHW FHGRISREES HRIIKQQGLV DGLFLLRDSQ
560 570 580 590 600
SNPKAFVLTL CHHQKIKNFQ ILPCEDDGQT FFTLDDGNTK FSDLIQLVDF
610 620
YQLNKGVLPC KLKHHCIRVA L
Length:621
Mass (Da):70,585
Last modified:January 4, 2005 - v2
Checksum:i6FC737E8F35468BB
GO
Isoform 2 (identifier: Q60760-2) [UniParc]FASTAAdd to Basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     117-141: Missing.

Note: Predominant isoform in most tissues.

Show »
Length:596
Mass (Da):67,543
Checksum:iEB13CA896DF41533
GO
Isoform 3 (identifier: Q60760-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-196: Missing.

Show »
Length:541
Mass (Da):61,218
Checksum:iA8FA9ED57C85F674
GO

Sequence cautioni

The sequence AAH53842.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAE37514.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti491 – 4922KR → NG in AAB53687. (PubMed:7731717)Curated
Sequence conflicti555 – 5551A → T in BAC28088. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei117 – 19680Missing in isoform 3. 1 PublicationVSP_012379Add
BLAST
Alternative sequencei117 – 14125Missing in isoform 2. 3 PublicationsVSP_001844Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18996 mRNA. Translation: AAB53687.1.
AF022072 mRNA. Translation: AAB72103.1.
AK030727 mRNA. Translation: BAC27100.1.
AK032927 mRNA. Translation: BAC28088.1.
AK163841 mRNA. Translation: BAE37514.1. Different initiation.
AL645803, AL663087 Genomic DNA. Translation: CAI23990.1.
AL645803, AL663087 Genomic DNA. Translation: CAI23991.1.
AL663087, AL645803 Genomic DNA. Translation: CAI25685.1.
AL663087, AL645803 Genomic DNA. Translation: CAI25687.1.
BC016111 mRNA. Translation: AAH16111.1.
BC053842 mRNA. Translation: AAH53842.1. Different initiation.
CCDSiCCDS24440.1. [Q60760-2]
CCDS48754.1. [Q60760-3]
PIRiI49199.
RefSeqiNP_001171100.1. NM_001177629.1. [Q60760-3]
NP_034475.2. NM_010345.4. [Q60760-2]
XP_006514592.1. XM_006514529.1. [Q60760-1]
UniGeneiMm.273117.
Mm.491389.

Genome annotation databases

EnsembliENSMUST00000093321; ENSMUSP00000091011; ENSMUSG00000020176. [Q60760-2]
ENSMUST00000109654; ENSMUSP00000105281; ENSMUSG00000020176. [Q60760-3]
GeneIDi14783.
KEGGimmu:14783.
UCSCiuc007iaz.2. mouse. [Q60760-3]
uc007iba.2. mouse. [Q60760-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18996 mRNA. Translation: AAB53687.1 .
AF022072 mRNA. Translation: AAB72103.1 .
AK030727 mRNA. Translation: BAC27100.1 .
AK032927 mRNA. Translation: BAC28088.1 .
AK163841 mRNA. Translation: BAE37514.1 . Different initiation.
AL645803 , AL663087 Genomic DNA. Translation: CAI23990.1 .
AL645803 , AL663087 Genomic DNA. Translation: CAI23991.1 .
AL663087 , AL645803 Genomic DNA. Translation: CAI25685.1 .
AL663087 , AL645803 Genomic DNA. Translation: CAI25687.1 .
BC016111 mRNA. Translation: AAH16111.1 .
BC053842 mRNA. Translation: AAH53842.1 . Different initiation.
CCDSi CCDS24440.1. [Q60760-2 ]
CCDS48754.1. [Q60760-3 ]
PIRi I49199.
RefSeqi NP_001171100.1. NM_001177629.1. [Q60760-3 ]
NP_034475.2. NM_010345.4. [Q60760-2 ]
XP_006514592.1. XM_006514529.1. [Q60760-1 ]
UniGenei Mm.273117.
Mm.491389.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3M7F X-ray 2.00 A 514-621 [» ]
ProteinModelPortali Q60760.
SMRi Q60760. Positions 195-437, 456-620.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200045. 6 interactions.
DIPi DIP-446N.
IntActi Q60760. 8 interactions.
MINTi MINT-102080.

PTM databases

PhosphoSitei Q60760.

Proteomic databases

MaxQBi Q60760.
PaxDbi Q60760.
PRIDEi Q60760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000093321 ; ENSMUSP00000091011 ; ENSMUSG00000020176 . [Q60760-2 ]
ENSMUST00000109654 ; ENSMUSP00000105281 ; ENSMUSG00000020176 . [Q60760-3 ]
GeneIDi 14783.
KEGGi mmu:14783.
UCSCi uc007iaz.2. mouse. [Q60760-3 ]
uc007iba.2. mouse. [Q60760-2 ]

Organism-specific databases

CTDi 2887.
MGIi MGI:103232. Grb10.

Phylogenomic databases

eggNOGi NOG307156.
GeneTreei ENSGT00550000074537.
HOVERGENi HBG000468.
InParanoidi Q60760.
OMAi ESTMGSE.
OrthoDBi EOG7SFHW7.
PhylomeDBi Q60760.
TreeFami TF317511.

Enzyme and pathway databases

Reactomei REACT_188578. Signaling by SCF-KIT.

Miscellaneous databases

ChiTaRSi GRB10. mouse.
NextBioi 286903.
PROi Q60760.
SOURCEi Search...

Gene expression databases

Bgeei Q60760.
CleanExi MM_GRB10.
ExpressionAtlasi Q60760. baseline and differential.
Genevestigatori Q60760.

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

« Hide 'large scale' publications
  1. "The cloning of Grb10 reveals a new family of SH2 domain proteins."
    Ooi J., Yajnik V., Immanuel D., Gordon M., Moskow J.J., Buchberg A., Margolis B.
    Oncogene 10:1621-1630(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EGFR, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Strain: Swiss.
  2. "The adapter protein Grb10 associates preferentially with the insulin receptor as compared with the IGF-I receptor in mouse fibroblasts."
    Laviola L., Giorgino F., Chow J.C., Baquero J.A., Hansen H., Ooi J., Zhu J., Riedel H., Smith R.J.
    J. Clin. Invest. 99:830-837(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH INSR AND IGF1R, TISSUE SPECIFICITY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Embryonic head.
  4. Griffiths C., Sycamore N.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    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] (ISOFORMS 2 AND 3).
    Tissue: Eye and Olfactory epithelium.
  6. "Identification of the Meg1/Grb10 imprinted gene on mouse proximal chromosome 11, a candidate for the Silver-Russell syndrome gene."
    Miyoshi N., Kuroiwa Y., Kohda T., Shitara H., Yonekawa H., Kawabe T., Hasegawa H., Barton S.C., Surani M.A., Kaneko-Ishino T., Ishino F.
    Proc. Natl. Acad. Sci. U.S.A. 95:1102-1107(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPRINTING, DEVELOPMENTAL STAGE.
  7. "Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
    Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
    Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR1; INSR; IGF1R; MET AND PDGFRB.
  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: IMPRINTING.
  9. "Two novel proteins that are linked to insulin-like growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling."
    Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.
    J. Biol. Chem. 278:31564-31573(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GIGYF1 AND GIGYF2.
  10. "The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor."
    Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.
    Mol. Cell. Biol. 23:3363-3372(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IGF1R AND NEDD4.
  11. "Disruption of the imprinted Grb10 gene leads to disproportionate overgrowth by an Igf2-independent mechanism."
    Charalambous M., Smith F.M., Bennett W.R., Crew T.E., Mackenzie F., Ward A.
    Proc. Natl. Acad. Sci. U.S.A. 100:8292-8297(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, IMPRINTING, DEVELOPMENTAL STAGE.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  13. "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 AKT1 AND YWHAE, PHOSPHORYLATION.
  14. "Distinct Grb10 domain requirements for effects on glucose uptake and insulin signaling."
    Mori K., Giovannone B., Smith R.J.
    Mol. Cell. Endocrinol. 230:39-50(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH INSR.
  15. "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, INTERACTION WITH LRP6.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization."
    Monami G., Emiliozzi V., Morrione A.
    J. Cell. Physiol. 216:426-437(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGRB10_MOUSE
AccessioniPrimary (citable) accession number: Q60760
Secondary accession number(s): O35352
, Q3TQ71, Q7TSA4, Q8BSH4, Q8BSS5, Q91WC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The GRB10 locus is imprinted. The maternal allele is expressed in most tissues, except the brain where it is expressed from the paternal allele. Expression from the maternal allele in fetal and adult brain was however described in PubMed:10861285.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3