Q60760 (GRB10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Growth factor receptor-bound protein 10

Alternative name(s):
GRB10 adapter protein
Maternally expressed gene 1 protein

Gene names

Name:	Grb10
Synonyms:	Meg1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.11 Ref.14 Ref.15 Ref.17
Enzyme regulation	Phosphorylation by mTORC1 stabilizes and activates GRB10 constituting a feedback pathway by which mTORC1 inhibits INSR-dependent signaling By similarity.
Subunit structure	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. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15
Subcellular location	Cytoplasm. 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. Ref.17
Tissue specificity	Widely expressed. Ref.1 Ref.2
Developmental stage	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. Ref.6 Ref.11
Domain	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.
Post-translational modification	Phosphorylated on serine residues upon EGF, FGF and PDGF stimulation. Ref.1 Ref.12 Ref.13 Ref.16
Disruption phenotype	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. Ref.11
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 Ref.8.
Sequence similarities	Belongs to the GRB7/10/14 family. Contains 1 PH domain. Contains 1 Ras-associating domain. Contains 1 SH2 domain.
Sequence caution	The sequence AAH53842.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE37514.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	insulin-like growth factor receptor signaling pathway Inferred from physical interaction Ref.9. Source: MGI negative regulation of Wnt receptor signaling pathway Inferred from direct assay Ref.15. Source: UniProtKB negative regulation of glucose import Inferred from mutant phenotype Ref.14. Source: BHF-UCL negative regulation of glycogen biosynthetic process Traceable author statement Ref.14. Source: BHF-UCL negative regulation of insulin receptor signaling pathway Inferred from mutant phenotype Ref.14. Source: BHF-UCL negative regulation of phosphorylation Inferred from direct assay Ref.14. Source: BHF-UCL positive regulation of vascular endothelial growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: MGI
Molecular function	SH3/SH2 adaptor activity Inferred from physical interaction Ref.14. Source: BHF-UCL insulin receptor binding Inferred from physical interaction Ref.14. Source: BHF-UCL phosphotyrosine binding Traceable author statement Ref.14. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nedd4	P46935	6	EBI-861810,EBI-773516

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q60760-1)

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.

Isoform 2 (identifier: Q60760-2)

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.

Isoform 3 (identifier: Q60760-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 621

621

Growth factor receptor-bound protein 10

PRO_0000150347

Regions

Domain

194 – 278

85

Ras-associating

Domain

318 – 427

110

PH

Domain

520 – 601

82

SH2

Amino acid modifications

Modified residue

50

1

Phosphoserine By similarity

Modified residue

96

1

Phosphoserine; by MTOR, MAPK1 and MAPK3 By similarity

Modified residue

432

1

Phosphotyrosine By similarity

Modified residue

455

1

Phosphoserine; by MTOR and PKB/AKT1 By similarity

Modified residue

458

1

Phosphoserine Ref.16

Modified residue

503

1

Phosphoserine; by MTOR, MAPK1 and MAPK3 By similarity

Natural variations

Alternative sequence

117 – 196

80

Missing in isoform 3.

VSP_012379

Alternative sequence

117 – 141

25

Missing in isoform 2.

VSP_001844

Experimental info

Sequence conflict

491 – 492

2

KR → NG in AAB53687. Ref.1

Sequence conflict

555

1

A → T in BAC28088. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

621

Helix Strand Turn

Details...

Helix

515 – 517

3

Helix

527 – 536

10

Beta strand

544 – 548

5

Beta strand

556 – 562

7

Beta strand

565 – 575

11

Beta strand

580 – 584

5

Beta strand

589 – 593

5

Helix

594 – 601

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 6FC737E8F35468BB	FASTA	621	70,585
	10 20 30 40 50 60 MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS PRQKMQRSQP 70 80 90 100 110 120 VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV APSSLPPPPS QPPAKHCGRC 130 140 150 160 170 180 EKWIPGENTR GNGKRKIWRW QFPPGFQLSK LTRPGLWTKT TARFSKKQPK NQCPTDTVNP 190 200 210 220 230 240 VARMPTSQME KLRLRKDVKV FSEDGTSKVV EILTDMTARD LCQLLVYKSH CVDDNSWTLV 250 260 270 280 290 300 EHHPQLGLER CLEDHEIVVQ VESTMPSESK FLFRKNYAKY EFFKNPVNFF PDQMVNWCQQ 310 320 330 340 350 360 SNGGQAQLLQ NFLNTSSCPE IQGFLQVKEV GRKSWKKLYV CLRRSGLYYS TKGTSKEPRH 370 380 390 400 410 420 LQLLADLEES SIFYLIAGKK QYNAPNEHGM CIKPNKAKTE MKELRLLCAE DEQIRTCWMT 430 440 450 460 470 480 AFRLLKYGML LYQNYRIPQR KGLPPPFNAP MRSVSENSLV AMDFSGQIGR VIDNPAEAQS 490 500 510 520 530 540 AALEEGHAWR KRSTRMNILS SQSPLHPSTL NAVIHRTQHW FHGRISREES HRIIKQQGLV 550 560 570 580 590 600 DGLFLLRDSQ SNPKAFVLTL CHHQKIKNFQ ILPCEDDGQT FFTLDDGNTK FSDLIQLVDF 610 620 YQLNKGVLPC KLKHHCIRVA L
	Isoform 2 (Delta) [UniParc]. Checksum: EB13CA896DF41533	FASTA	596	67,543
	10 20 30 40 50 60 MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS PRQKMQRSQP 70 80 90 100 110 120 VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV APSSLPPPPS QPPAKHFPPG 130 140 150 160 170 180 FQLSKLTRPG LWTKTTARFS KKQPKNQCPT DTVNPVARMP TSQMEKLRLR KDVKVFSEDG 190 200 210 220 230 240 TSKVVEILTD MTARDLCQLL VYKSHCVDDN SWTLVEHHPQ LGLERCLEDH EIVVQVESTM 250 260 270 280 290 300 PSESKFLFRK NYAKYEFFKN PVNFFPDQMV NWCQQSNGGQ AQLLQNFLNT SSCPEIQGFL 310 320 330 340 350 360 QVKEVGRKSW KKLYVCLRRS GLYYSTKGTS KEPRHLQLLA DLEESSIFYL IAGKKQYNAP 370 380 390 400 410 420 NEHGMCIKPN KAKTEMKELR LLCAEDEQIR TCWMTAFRLL KYGMLLYQNY RIPQRKGLPP 430 440 450 460 470 480 PFNAPMRSVS ENSLVAMDFS GQIGRVIDNP AEAQSAALEE GHAWRKRSTR MNILSSQSPL 490 500 510 520 530 540 HPSTLNAVIH RTQHWFHGRI SREESHRIIK QQGLVDGLFL LRDSQSNPKA FVLTLCHHQK 550 560 570 580 590 IKNFQILPCE DDGQTFFTLD DGNTKFSDLI QLVDFYQLNK GVLPCKLKHH CIRVAL
	Isoform 3 [UniParc]. Checksum: A8FA9ED57C85F674	FASTA	541	61,218
	10 20 30 40 50 60 MNNDINSSVE SLNSACNMQS DTDTAPLLED GQHASNQGAA SSSRGQPQAS PRQKMQRSQP 70 80 90 100 110 120 VHILRRLQEE DQQLRTASLP AIPNPFPELT GAAPGSPPSV APSSLPPPPS QPPAKHDVKV 130 140 150 160 170 180 FSEDGTSKVV EILTDMTARD LCQLLVYKSH CVDDNSWTLV EHHPQLGLER CLEDHEIVVQ 190 200 210 220 230 240 VESTMPSESK FLFRKNYAKY EFFKNPVNFF PDQMVNWCQQ SNGGQAQLLQ NFLNTSSCPE 250 260 270 280 290 300 IQGFLQVKEV GRKSWKKLYV CLRRSGLYYS TKGTSKEPRH LQLLADLEES SIFYLIAGKK 310 320 330 340 350 360 QYNAPNEHGM CIKPNKAKTE MKELRLLCAE DEQIRTCWMT AFRLLKYGML LYQNYRIPQR 370 380 390 400 410 420 KGLPPPFNAP MRSVSENSLV AMDFSGQIGR VIDNPAEAQS AALEEGHAWR KRSTRMNILS 430 440 450 460 470 480 SQSPLHPSTL NAVIHRTQHW FHGRISREES HRIIKQQGLV DGLFLLRDSQ SNPKAFVLTL 490 500 510 520 530 540 CHHQKIKNFQ ILPCEDDGQT FFTLDDGNTK FSDLIQLVDF YQLNKGVLPC KLKHHCIRVA L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7731717] [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: 9062339] [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: 16141072] [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: 15489334] [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: 9448292] [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: 10454568] [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: 10861285] [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: 12771153] [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: 12697834] [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: 12829789] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, IMPRINTING, DEVELOPMENTAL STAGE.
[12]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, MASS SPECTROMETRY. 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: 15722337] [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: 15664450] [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: 17376403] [Abstract] Cited for: FUNCTION, INTERACTION WITH LRP6.
[16]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY. 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: 18286479] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00127976.
IPI00331684.
IPI00473353.

PIR

I49199.

RefSeq

NP_001171100.1. NM_001177629.1.
NP_034475.2. NM_010345.4.

UniGene

Mm.273117.
Mm.464229.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M7F	X-ray	2.00	A	514-621	[»]

ProteinModelPortal

Q60760.

SMR

Q60760. Positions 195-437, 456-620.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-446N.

IntAct

Q60760. 1 interaction.

MINT

MINT-102080.

STRING

Q60760.

PTM databases

PhosphoSite

Q60760.

Proteomic databases

PRIDE

Q60760.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000078449; ENSMUSP00000077544; ENSMUSG00000020176.
ENSMUST00000093321; ENSMUSP00000091011; ENSMUSG00000020176.
ENSMUST00000109654; ENSMUSP00000105281; ENSMUSG00000020176.
ENSMUST00000109656; ENSMUSP00000105283; ENSMUSG00000020176.

GeneID

14783.

KEGG

mmu:14783.

NMPDR

fig|10090.3.peg.23293.

UCSC

uc007iaz.2. mouse.
uc007iba.2. mouse.

Organism-specific databases

CTD

2887.

MGI

MGI:103232. Grb10.

Phylogenomic databases

eggNOG

maNOG04054.

HOGENOM

HBG358659.

HOVERGEN

HBG000468.

InParanoid

Q60760.

OMA

STRMNIL.

PhylomeDB

Q60760.

Gene expression databases

ArrayExpress

Q60760.

Bgee

Q60760.

CleanEx

MM_GRB10.

Genevestigator

Q60760.

GermOnline

ENSMUSG00000020176. Mus musculus.

Family and domain databases

InterPro

IPR015042. BPS-dom.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000159. Ras-assoc.
IPR000980. SH2.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF08947. BPS. 1 hit.
PF00169. PH. 1 hit.
PF00788. RA. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.

SMART

SM00233. PH. 1 hit.
SM00314. RA. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]

PROSITE

PS50003. PH_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

GRB10_MOUSE

Accession

Primary (citable) accession number: Q60760
Secondary accession number(s): O35352 , Q3TQ71, Q7TSA4, Q8BSH4, Q8BSS5, Q91WC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program