P98083 (SHC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SHC-transforming protein 1

Alternative name(s):
SHC-transforming protein A
Src homology 2 domain-containing-transforming protein C1
Short name=SH2 domain protein C1

Gene names

Name:	Shc1
Synonyms:	Shc, ShcA

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis By similarity. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p47Shc and isoform p52Shc, once phosphorylated, couple activated receptor kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p47Shc and isoform p52 may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span. Ref.18 Ref.21
Subunit structure	Interacts with the NPXY motif of tyrosine-phosphorylated IGF1R and INSR in vitro via the PID domain. Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated DDR2 and CD3T. Interacts with the N-terminal region of APS. Interacts with GRB7 and KIT By similarity. Interacts with PTK2/FAK1 By similarity. Interacts with phosphorylated LRP1 and IRS4. Interacts with FLT4 (tyrosine-phosphorylated) By similarity. Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4 By similarity. Interacts with TEK/TIE2 (tyrosine-phosphorylated) By similarity. Interacts with ALK, GAB2, TRIM31, INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.23
Subcellular location	Cytoplasm By similarity Ref.21. Isoform p47Shc: Mitochondrion matrix By similarity. Note: Targeting of isoform p47Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization By similarity. Ref.21 Isoform p66Shc: Mitochondrion. Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation. Ref.21
Tissue specificity	Widely expressed. Expressed in neural stem cells but absent in mature neurons.
Domain	In response to a variety of growth factors, isoform p47Shc and isoform p52 bind to phosphorylated receptors through their phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2 domains bind to specific phosphorylated tyrosine residues in the Asn-Pro-Xaa-Tyr(P) motif. Isoform p47Shc and isoform p52Shc are in turn phosphorylated on three tyrosine residues within the extended proline-rich domain. These phosphotyrosines act as docking site for GRB2 and thereby are involved in Ras activation.
Post-translational modification	Phosphorylated in response to FLT4 signaling By similarity. Tyrosine phosphorylated by ligand-activated PDGFRB By similarity. May be tyrosine phosphorylated by activated PTK2/FAK1 By similarity. Tyrosine phosphorylated by TEK/TIE2 By similarity. Tyrosine phosphorylated by activated PTK2B/PYK2 By similarity. Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to KIT signaling. Isoform p47Shc and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36 by PRKCB upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light. FLT3 signaling promotes tyrosine phosphorylation of isoform p47Shc and isoform p52Shc. Also tyrosine phosphorylated by ligand-activated ALK. Ref.8 Ref.14 Ref.21
Sequence similarities	Contains 1 PID domain. Contains 1 SH2 domain.

Ontologies

Keywords
Biological process	Angiogenesis Growth regulation
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation Alternative splicing
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from sequence or structural similarity. Source: UniProtKB actin cytoskeleton reorganization Inferred from mutant phenotype PubMed 10809671. Source: MGI activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB angiogenesis Inferred from mutant phenotype PubMed 10809671. Source: MGI cell-cell adhesion Inferred from mutant phenotype PubMed 10809671. Source: MGI heart development Inferred from mutant phenotype PubMed 10809671. Source: MGI regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Amd1	P31154	7	EBI-300201,EBI-644529
Shcbp1	Q9Z179	5	EBI-300201,EBI-644352

Alternative products

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

Note: In human, it is alternative promoter usage that produces such isoforms.

Isoform p66Shc (identifier: P98083-1)

Also known as: p66;

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 p52Shc (identifier: P98083-2)

Also known as: p52;

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.

Note: Produced by alternative splicing.

Isoform p47Shc (identifier: P98083-3)

Also known as: p47;

The sequence of this isoform differs from the canonical sequence as follows:
     1-155: Missing.

Note: Produced by alternative initiation at Met-46 of isoform p52.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 579	579	SHC-transforming protein 1		PRO_0000022339
Regions
	Domain	156 – 339	184	PID
	Domain	484 – 575	92	SH2
	Region	340 – 483	144	CH1
	Compositional bias	408 – 470	63	Pro-rich
Amino acid modifications
	Modified residue	36	1	Phosphoserine; in isoform p66Shc Ref.8 Ref.21
	Modified residue	139	1	Phosphoserine Ref.24
	Modified residue	349	1	Phosphotyrosine Ref.19
	Modified residue	350	1	Phosphotyrosine Ref.19
	Modified residue	422	1	Phosphoserine By similarity
	Modified residue	423	1	Phosphotyrosine Ref.19 Ref.20 Ref.22
Natural variations
	Alternative sequence	1 – 155	155	Missing in isoform p47Shc.		VSP_018792
	Alternative sequence	1 – 110	110	Missing in isoform p52Shc.		VSP_018791

Sequences

	Sequence		Length	Mass (Da)
	Isoform p66Shc (p66) [UniParc]. Last modified May 27, 2002. Version 3. Checksum: 99C22E64412B6236	FASTA	579	62,608
	10 20 30 40 50 60 MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS 70 80 90 100 110 120 FFPRMSNLKL ANPAGGRLGP KGEPGKAAED GEGSAGAALR DSGLLPLLQD MNKLSGGGGR 130 140 150 160 170 180 RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV EVLQSMRALD 190 200 210 220 230 240 FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS 250 260 270 280 290 300 LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV 310 320 330 340 350 360 ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY NDFPGKEPPL 370 380 390 400 410 420 GGVVDMRLRE GAARPTLPSA QMSSHLGATL PIGQHAAGDH EVRKQMLPPP PCPGRELFDD 430 440 450 460 470 480 PSYVNIQNLD KARQAGGGAG PPNPSLNGSA PRDLFDMKPF EDALRVPPPP QSMSMAEQLQ 490 500 510 520 530 540 GEPWFHGKLS RREAEALLQL NGDFLVREST TTPGQYVLTG LQSGQPKHLL LVDPEGVVRT 550 560 570 KDHRFESVSH LISYHMDNHL PIISAGSELC LQQPVDRKV
	Isoform p52Shc (p52) [UniParc]. Checksum: DF33594E80107A3E	FASTA	469	51,409
	10 20 30 40 50 60 MNKLSGGGGR RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV 70 80 90 100 110 120 EVLQSMRALD FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM 130 140 150 160 170 180 PITLTVSTSS LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL 190 200 210 220 230 240 ECPEGLAQDV ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY 250 260 270 280 290 300 NDFPGKEPPL GGVVDMRLRE GAARPTLPSA QMSSHLGATL PIGQHAAGDH EVRKQMLPPP 310 320 330 340 350 360 PCPGRELFDD PSYVNIQNLD KARQAGGGAG PPNPSLNGSA PRDLFDMKPF EDALRVPPPP 370 380 390 400 410 420 QSMSMAEQLQ GEPWFHGKLS RREAEALLQL NGDFLVREST TTPGQYVLTG LQSGQPKHLL 430 440 450 460 LVDPEGVVRT KDHRFESVSH LISYHMDNHL PIISAGSELC LQQPVDRKV
	Isoform p47Shc (p47) [UniParc]. Checksum: 5064FFF6CE5BD930	FASTA	424	46,467
	10 20 30 40 50 60 MGPGVSYLVR YMGCVEVLQS MRALDFNTRT QVTREAISLV CEAVPGAKGA TRRRKPCSRP 70 80 90 100 110 120 LSSILGRSNL KFAGMPITLT VSTSSLNLMA ADCKQIIANH HMQSISFASG GDPDTAEYVA 130 140 150 160 170 180 YVAKDPVNQR ACHILECPEG LAQDVISTIG QAFELRFKQY LRNPPKLVTP HDRMAGFDGS 190 200 210 220 230 240 AWDEEEEEPP DHQYYNDFPG KEPPLGGVVD MRLREGAARP TLPSAQMSSH LGATLPIGQH 250 260 270 280 290 300 AAGDHEVRKQ MLPPPPCPGR ELFDDPSYVN IQNLDKARQA GGGAGPPNPS LNGSAPRDLF 310 320 330 340 350 360 DMKPFEDALR VPPPPQSMSM AEQLQGEPWF HGKLSRREAE ALLQLNGDFL VRESTTTPGQ 370 380 390 400 410 420 YVLTGLQSGQ PKHLLLVDPE GVVRTKDHRF ESVSHLISYH MDNHLPIISA GSELCLQQPV DRKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Blaikie P.A., Yajnik V., Margolis B. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM P66SHC).
[2]	"A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors." Blaikie P.A., Immanuel D., Wu J., Li N., Yajnik V., Margolis B. J. Biol. Chem. 269:32031-32034(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P52SHC).
[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] (ISOFORMS P52SHC AND P66SHC). Strain: C57BL/6J and NOD.
[4]	"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 P52SHC). Strain: FVB/N. Tissue: Colon.
[5]	"The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter." Ventura A., Luzi L., Pacini S., Baldari C.T., Pelicci P.-G. J. Biol. Chem. 277:22370-22376(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-165 (ISOFORMS P66SHC AND P52SHC). Strain: 129/SvJ.
[6]	"p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity." Lioubin M.N., Algate P.A., Tsai S., Carlberg K., Aebersold A., Rohrschneider L.R. Genes Dev. 10:1084-1095(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[7]	"The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase." Damen J.E., Liu L., Rosten P., Humphries R.K., Jefferson A.B., Majerus P.W., Krystal G. Proc. Natl. Acad. Sci. U.S.A. 93:1689-1693(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[8]	"Insulin stimulates the phosphorylation of the 66- and 52-kilodalton Shc isoforms by distinct pathways." Kao A.W., Waters S.B., Okada S., Pessin J.E. Endocrinology 138:2474-2480(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-36.
[9]	"The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis." Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., Krystal G. J. Biol. Chem. 272:8983-8988(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[10]	"Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP." Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G., Ravichandran K.S. J. Biol. Chem. 272:10396-10401(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPPL1.
[11]	"Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation." Gu H., Pratt J.C., Burakoff S.J., Neel B.G. Mol. Cell 2:729-740(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAB2.
[12]	"Role of SHIP in FcgammaRIIb-mediated inhibition of Ras activation in B cells." Tridandapani S., Phee H., Shivakumar L., Kelley T.W., Coggeshall K.M. Mol. Immunol. 35:1135-1146(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[13]	"A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development." Lucas D.M., Rohrschneider L.R. Blood 93:1922-1933(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[14]	"Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells." Zhang S., Mantel C., Broxmeyer H.E. J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING, INTERACTION WITH GRB2 AND PTPN6/SHP.
[15]	"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling." Cavallaro U., Niedermeyer J., Fuxa M., Christofori G. Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; SHC1; FGFR4 AND CTTN.
[16]	"Mechanism of TrkB-mediated hippocampal long-term potentiation." Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M. Neuron 36:121-137(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NTRK2.
[17]	"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis." Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U. J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHB1 AND GRB2.
[18]	"Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet." Napoli C., Martin-Padura I., de Nigris F., Giorgio M., Mansueto G., Somma P., Condorelli M., Sica G., De Rosa G., Pelicci P.-G. Proc. Natl. Acad. Sci. U.S.A. 100:2112-2116(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349; TYR-350 AND TYR-423, MASS SPECTROMETRY.
[20]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-423, MASS SPECTROMETRY. Tissue: Mast cell.
[21]	"Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc." Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E., Giorgio M., Contursi C., Minucci S., Mantovani F., Wieckowski M.R., Del Sal G., Pelicci P.G., Rizzuto R. Science 315:659-663(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORM P66SHC), PHOSPHORYLATION AT SER-36 (ISOFORM P66SHC).
[22]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-423, MASS SPECTROMETRY. Tissue: Brain.
[23]	"TRIM31 interacts with p52(Shc) and inhibits Src-induced anchorage-independent growth." Watanabe M., Tsukiyama T., Hatakeyama S. Biochem. Biophys. Res. Commun. 388:422-427(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM31.
[24]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U46956 Genomic DNA. Translation: AAA91777.2. U15784 mRNA. Translation: AAC52146.1. AK049357 mRNA. Translation: BAC33706.1. AK155158 mRNA. Translation: BAE33083.1. BC036172 mRNA. Translation: AAH36172.1. AF455140 Genomic DNA. Translation: AAM61857.1. AF455140 Genomic DNA. Translation: AAM61858.1.
IPI	IPI00125298. IPI00759853. IPI00759982.
PIR	A55484.
RefSeq	NP_001106802.1. NM_001113331.2. NP_035498.2. NM_011368.5.
UniGene	Mm.86595.
3D structure databases
ProteinModelPortal	P98083.
SMR	P98083. Positions 111-317, 478-579.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-271N. DIP-29912N.
IntAct	P98083. 16 interactions.
MINT	MINT-127650.
PTM databases
PhosphoSite	P98083.
Proteomic databases
PaxDb	P98083.
PRIDE	P98083.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000039110; ENSMUSP00000035361; ENSMUSG00000042626. ENSMUST00000094378; ENSMUSP00000091940; ENSMUSG00000042626. ENSMUST00000107417; ENSMUSP00000103040; ENSMUSG00000042626.
GeneID	20416.
KEGG	mmu:20416.
UCSC	uc008pzm.2. mouse. uc008pzn.2. mouse.
Organism-specific databases
CTD	6464.
MGI	MGI:98296. Shc1.
Phylogenomic databases
eggNOG	NOG315087.
GeneTree	ENSGT00390000018860.
HOGENOM	HOG000231974.
HOVERGEN	HBG050121.
InParanoid	P98083.
KO	K06279.
OMA	NPAVNGS.
OrthoDB	EOG42NJ0D.
Gene expression databases
ArrayExpress	P98083.
Bgee	P98083.
Genevestigator	P98083.
GermOnline	ENSMUSG00000042626. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR006019. PID_domain. IPR006020. PTyr_interaction_dom. IPR000980. SH2. [Graphical view]
Pfam	PF00640. PID. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00629. SHCPIDOMAIN.
SMART	SM00462. PTB. 1 hit. SM00252. SH2. 1 hit. [Graphical view]
PROSITE	PS01179. PID. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SHC1. mouse.
NextBio	298412.
SOURCE	Search...

Entry information

Entry name

SHC1_MOUSE

Accession

Primary (citable) accession number: P98083
Secondary accession number(s): Q3U2Q7 , Q8BFY3, Q8K4C6, Q8K4C7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	May 27, 2002
Last modified:	April 3, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program