P29353 (SHC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SHC-transforming protein 1

Alternative name(s):
SHC-transforming protein 3
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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	583 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 a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc 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 By similarity. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis. Ref.31
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 CD3T and DDR2. Interacts with the N-terminal region of APS. Interacts with phosphorylated LRP1 and IRS4. Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with TRIM31. Interacts with PTPN6/SHP (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTT By similarity. Interacts with ALK, GAB2, GRB7 and KIT. Interacts with FLT4 (tyrosine-phosphorylated). Interacts with EPHB1 and GRB2; activates the MAPK/ERK cascade to regulate cell migration. Interacts with PDGFRB (tyrosine-phosphorylated). Interacts with ERBB4. Interacts with TEK/TIE2 (tyrosine-phosphorylated). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; in a phosphotyrosine-dependent manner. Interacts with PTK2/FAK1. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.35 Ref.39 Ref.40
Subcellular location	Cytoplasm Ref.34. Isoform p46Shc: Mitochondrion matrix. Note: Localized to the mitochondria matrix. Targeting of isoform p46Shc 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. Ref.34 Isoform p66Shc: Mitochondrion By similarity. Note: In case of oxidative conditions, phosphorylation at 'Ser-36' of isoform p66Shc, leads to mitochondrial accumulation By similarity. Ref.34
Tissue specificity	Widely expressed. Expressed in neural stem cells but absent in mature neurons.
Domain	In response to a variety of growth factors, isoform p46Shc and isoform p52Shc bind to phosphorylated Trk 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 of the Trk receptors. Isoform p46Shc 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 By similarity.
Post-translational modification	Phosphorylated by activated epidermal growth factor receptor. Phosphorylated in response to FLT4 and KIT signaling. Isoform p46Shc 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 By similarity. Tyrosine phosphorylated in response to FLT3 signaling By similarity. Tyrosine phosphorylated by activated PTK2B/PYK2 By similarity. Tyrosine phosphorylated by ligand-activated ALK. Tyrosine phosphorylated by ligand-activated PDGFRB. Tyrosine phosphorylated by TEK/TIE2. May be tyrosine phosphorylated by activated PTK2/FAK1; tyrosine phosphorylation was seen in an astrocytoma biopsy, where PTK2/FAK1 kinase activity is high, but not in normal brain tissue. Ref.9 Ref.15 Ref.18 Ref.19 Ref.22 Ref.26 Ref.30 Ref.31 Ref.36 Ref.39
Sequence similarities	Contains 1 PID domain. Contains 1 SH2 domain.
Sequence caution	The sequence CAI13254.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Angiogenesis Growth regulation
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from direct assay PubMed 14676841. Source: UniProtKB Ras protein signal transduction Traceable author statement. Source: Reactome actin cytoskeleton reorganization Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from direct assay PubMed 14676841. Source: UniProtKB activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell-cell adhesion Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome heart development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL leukocyte migration Traceable author statement. Source: Reactome neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome positive regulation of DNA replication Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cell proliferation Non-traceable author statement PubMed 14676841. Source: UniProtKB regulation of epidermal growth factor-activated receptor activity Traceable author statement Ref.1. Source: ProtInc regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Shc-EGFR complex Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	epidermal growth factor receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL phospholipid binding Traceable author statement PubMed 14676841. Source: UniProtKB protein tyrosine kinase activity Traceable author statement. Source: Reactome transmembrane receptor protein tyrosine kinase adaptor activity Traceable author statement PubMed 14676841. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	5	EBI-78835,EBI-77613
EGFR	P00533	5	EBI-78835,EBI-297353
ESR1	P03372-4	2	EBI-78835,EBI-4309277
GRB2	P62993	8	EBI-78835,EBI-401755
IGF1R	P08069	2	EBI-1000553,EBI-475981

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform p66Shc (identifier: P29353-1)

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.

Note: Regulated by epigenetic modifications of its promoter region.

Isoform p52Shc (identifier: P29353-2)

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

Isoform p46Shc (identifier: P29353-3)

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

Isoform 5 (identifier: P29353-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-214: Missing.
     215-221: PLSSILG → MSLCHRW

Note: Produced by alternative splicing.

Isoform 6 (identifier: P29353-6)

The sequence of this isoform differs from the canonical sequence as follows:
     417-417: P → PA

Note: Produced by alternative splicing.

Isoform 7 (identifier: P29353-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
     417-417: P → PA

Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 583

583

SHC-transforming protein 1

PRO_0000097731

Regions

Domain

156 – 339

184

PID

Domain

488 – 579

92

SH2

Region

340 – 487

148

CH1

Compositional bias

411 – 474

64

Pro-rich

Amino acid modifications

Modified residue

36

1

Phosphoserine Ref.36

Modified residue

139

1

Phosphoserine Ref.38 Ref.41 Ref.46

Modified residue

349

1

Phosphotyrosine Ref.15 Ref.19 Ref.22

Modified residue

350

1

Phosphotyrosine Ref.15 Ref.19 Ref.22

Modified residue

426

1

Phosphoserine

Modified residue

427

1

Phosphotyrosine Ref.19 Ref.22 Ref.41 Ref.43

Natural variations

Alternative sequence

1 – 214

214

Missing in isoform 5.

VSP_040090

Alternative sequence

1 – 155

155

Missing in isoform p46Shc.

VSP_016107

Alternative sequence

1 – 110

110

Missing in isoform p52Shc and isoform 7.

VSP_016108

Alternative sequence

215 – 221

7

PLSSILG → MSLCHRW in isoform 5.

VSP_040091

Alternative sequence

417

1

P → PA in isoform 7 and isoform 6.

VSP_040092

Natural variant

205

1

A → V.
Corresponds to variant rs8191981 [ dbSNP | Ensembl ].

VAR_042428

Natural variant

410

1

M → V.
Corresponds to variant rs8191979 [ dbSNP | Ensembl ].

VAR_051353

Experimental info

Sequence conflict

2

1

D → N in CAA70977. Ref.3

Sequence conflict

21

1

L → M in CAA70977. Ref.3

Sequence conflict

38

1

S → P in CAA70977. Ref.3

Sequence conflict

95

1

V → D in AAB49972. Ref.2

Sequence conflict

101

1

D → E in AAB49972. Ref.2

Sequence conflict

430

1

V → A in BAG70069. Ref.5

Sequence conflict

430

1

V → A in BAG70193. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

583

Helix Strand Turn

Details...

Beta strand

113 – 115

3

Beta strand

142 – 145

4

Beta strand

148 – 150

3

Helix

152 – 156

5

Beta strand

160 – 167

8

Beta strand

169 – 171

3

Turn

176 – 178

3

Beta strand

179 – 181

3

Helix

184 – 198

15

Helix

200 – 202

3

Beta strand

206 – 208

3

Beta strand

215 – 218

4

Beta strand

222 – 224

3

Beta strand

229 – 237

9

Beta strand

240 – 245

6

Turn

246 – 249

4

Beta strand

251 – 255

5

Beta strand

256 – 259

4

Beta strand

261 – 263

3

Beta strand

265 – 267

3

Beta strand

270 – 272

3

Beta strand

274 – 278

5

Beta strand

281 – 283

3

Beta strand

286 – 291

6

Beta strand

293 – 295

3

Helix

297 – 302

6

Beta strand

311 – 314

4

Turn

483 – 485

3

Beta strand

487 – 489

3

Helix

495 – 499

5

Beta strand

507 – 512

6

Beta strand

514 – 516

3

Beta strand

518 – 526

9

Beta strand

529 – 536

8

Beta strand

540 – 543

4

Beta strand

548 – 551

4

Helix

552 – 562

11

Beta strand

566 – 568

3

Beta strand

571 – 573

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform p66Shc [UniParc]. Last modified April 8, 2008. Version 4. Checksum: 7EFA5CB185A548D1	FASTA	583	62,822
	10 20 30 40 50 60 MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS 70 80 90 100 110 120 FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP DSGPLPLLQD 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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPGRE 430 440 450 460 470 480 LFDDPSYVNV QNLDKARQAV GGAGPPNPAI NGSAPRDLFD MKPFEDALRV PPPPQSVSMA 490 500 510 520 530 540 EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG 550 560 570 580 VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL
	Isoform p52Shc [UniParc]. Checksum: 6DDC519E3F318B6D	FASTA	473	51,611
	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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM 310 320 330 340 350 360 PPPPPCPGRE LFDDPSYVNV QNLDKARQAV GGAGPPNPAI NGSAPRDLFD MKPFEDALRV 370 380 390 400 410 420 PPPPQSVSMA EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP 430 440 450 460 470 KHLLLVDPEG VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL
	Isoform p46Shc [UniParc]. Checksum: 099FED4690662DD5	FASTA	428	46,668
	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 MRLREGAAPG AARPTAPNAQ TPSHLGATLP 250 260 270 280 290 300 VGQPVGGDPE VRKQMPPPPP CPGRELFDDP SYVNVQNLDK ARQAVGGAGP PNPAINGSAP 310 320 330 340 350 360 RDLFDMKPFE DALRVPPPPQ SVSMAEQLRG EPWFHGKLSR REAEALLQLN GDFLVRESTT 370 380 390 400 410 420 TPGQYVLTGL QSGQPKHLLL VDPEGVVRTK DHRFESVSHL ISYHMDNHLP IISAGSELCL QQPVERKL
	Isoform 5 [UniParc]. Checksum: 46F34449B556DDD0	FASTA	369	40,415
	10 20 30 40 50 60 MSLCHRWRSN LKFAGMPITL TVSTSSLNLM AADCKQIIAN HHMQSISFAS GGDPDTAEYV 70 80 90 100 110 120 AYVAKDPVNQ RACHILECPE GLAQDVISTI GQAFELRFKQ YLRNPPKLVT PHDRMAGFDG 130 140 150 160 170 180 SAWDEEEEEP PDHQYYNDFP GKEPPLGGVV DMRLREGAAP GAARPTAPNA QTPSHLGATL 190 200 210 220 230 240 PVGQPVGGDP EVRKQMPPPP PCPGRELFDD PSYVNVQNLD KARQAVGGAG PPNPAINGSA 250 260 270 280 290 300 PRDLFDMKPF EDALRVPPPP QSVSMAEQLR GEPWFHGKLS RREAEALLQL NGDFLVREST 310 320 330 340 350 360 TTPGQYVLTG LQSGQPKHLL LVDPEGVVRT KDHRFESVSH LISYHMDNHL PIISAGSELC LQQPVERKL
	Isoform 6 [UniParc]. Checksum: BDB2FF81953D4FF4	FASTA	584	62,893
	10 20 30 40 50 60 MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS 70 80 90 100 110 120 FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIVGAAMP DSGPLPLLQD 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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPAGR 430 440 450 460 470 480 ELFDDPSYVN VQNLDKARQA VGGAGPPNPA INGSAPRDLF DMKPFEDALR VPPPPQSVSM 490 500 510 520 530 540 AEQLRGEPWF HGKLSRREAE ALLQLNGDFL VRESTTTPGQ YVLTGLQSGQ PKHLLLVDPE 550 560 570 580 GVVRTKDHRF ESVSHLISYH MDNHLPIISA GSELCLQQPV ERKL
	Isoform 7 [UniParc]. Checksum: 43E1D98CBA87DB37	FASTA	474	51,682
	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 GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM 310 320 330 340 350 360 PPPPPCPAGR ELFDDPSYVN VQNLDKARQA VGGAGPPNPA INGSAPRDLF DMKPFEDALR 370 380 390 400 410 420 VPPPPQSVSM AEQLRGEPWF HGKLSRREAE ALLQLNGDFL VRESTTTPGQ YVLTGLQSGQ 430 440 450 460 470 PKHLLLVDPE GVVRTKDHRF ESVSHLISYH MDNHLPIISA GSELCLQQPV ERKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction." Pelicci G., Lanfrancone L., Grignani F., McGlade J., Cavallo F., Forni G., Nicoletti I., Grignani F., Pawson T., Pelicci P.-G. Cell 70:93-104(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P46SHC AND P52SHC).
[2]	"Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway." Migliaccio E., Mele S., Salcini A.E., Pelicci G., Lai K.M., Superti-Furga G., Pawson T., Di Fiore P.P., Lanfrancone L., Pelicci P.-G. EMBO J. 16:706-716(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P66SHC).
[3]	"Characterization of human SHC p66 cDNA and its processed pseudogene mapping to Xq12-q13.1." Harun R.B., Smith K.K., Leek J.P., Markham A.F., Norris A., Morrison J.F. Genomics 42:349-352(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Fibroblast.
[4]	"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 P52SHC). Tissue: Mammary gland and Synovium.
[5]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 P52SHC AND 7). Tissue: Choriocarcinoma and Neuroblastoma.
[9]	"Direct interaction between Shc and the platelet-derived growth factor beta-receptor." Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H., Claesson-Welsh L. J. Biol. Chem. 269:15337-15343(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDGFRB AND GRB2, PHOSPHORYLATION.
[10]	"Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses." Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., Kaplan D.R. Neuron 12:691-705(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NTRK1.
[11]	"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor." Craparo A., O'Neill T.J., Gustafson T.A. J. Biol. Chem. 270:15639-15643(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGF1R.
[12]	"Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains." He W., O'Neill T.J., Gustafson T.A. J. Biol. Chem. 270:23258-23262(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INSR.
[13]	"Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain." Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J. Mol. Cell. Biol. 15:2500-2508(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INSR.
[14]	"Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation." Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., Krystal G. Blood 88:2833-2840(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D.
[15]	"The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions." van der Geer P., Wiley S., Gish G.D., Pawson T. Curr. Biol. 6:1435-1444(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-349 AND TYR-350.
[16]	"Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors." Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L. J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7.
[17]	"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes." Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H. J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIT.
[18]	"Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src." Schlaepfer D.D., Hunter T. J. Biol. Chem. 272:13189-13195(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[19]	"Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activation." Gotoh N., Toyoda M., Shibuya M. Mol. Cell. Biol. 17:1824-1831(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
[20]	"Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation." Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A., Yoshimura A. Oncogene 15:7-15(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APS.
[21]	"Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein." Habib T., Hejna J.A., Moses R.E., Decker S.J. J. Biol. Chem. 273:18605-18609(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPP5D AND INPPL1.
[22]	"Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events." Schlaepfer D.D., Jones K.C., Hunter T. Mol. Cell. Biol. 18:2571-2585(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-349; TYR-350 AND TYR-427.
[23]	"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells." Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B. Blood 93:2707-2720(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPPL1.
[24]	"Ligand discrimination in signaling through an ErbB4 receptor homodimer." Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., Carraway K.L. III J. Biol. Chem. 275:19803-19807(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERBB4.
[25]	"The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells." Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S., Moreau C., Payrastre B., Erneux C. J. Biol. Chem. 276:28348-28355(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPPL1.
[26]	"Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples." Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart J. Jr., Gladson C.L. Cancer Res. 62:2699-2707(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION.
[27]	"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: ALTERNATIVE PROMOTER USAGE.
[28]	"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.
[29]	"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma." Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R. Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NTRK1.
[30]	"Signal transduction via the stem cell factor receptor/c-Kit." Ronnstrand L. Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN KIT SIGNALING, PHOSPHORYLATION.
[31]	"Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and regulates migration and sprouting but not survival of endothelial cells." Audero E., Cascone I., Maniero F., Napione L., Arese M., Lanfrancone L., Bussolino F. J. Biol. Chem. 279:13224-13233(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH TEK.
[32]	"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress." Wang J.F., Zhang X., Groopman J.E. J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLT4.
[33]	"Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4." Hinsby A.M., Olsen J.V., Mann M. J. Biol. Chem. 279:46438-46447(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IRS4.
[34]	"A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria." Ventura A., Maccarana M., Raker V.A., Pelicci P.-G. J. Biol. Chem. 279:2299-2306(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION (ISOFORM P46SHC).
[35]	"Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules." Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K. J. Biol. Chem. 279:40536-40544(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRP1.
[36]	"Phosphorylation of p66Shc and forkhead proteins mediates Abeta toxicity." Smith W.W., Norton D.D., Gorospe M., Jiang H., Nemoto S., Holbrook N.J., Finkel T., Kusiak J.W. J. Cell Biol. 169:331-339(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-36.
[37]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[39]	"ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation." Degoutin J., Vigny M., Gouzi J.Y. FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALK, PHOSPHORYLATION.
[40]	"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein." Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J. EMBO J. 27:2305-2316(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAB2.
[41]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND TYR-427, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[44]	"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.
[45]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY.
[47]	"Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data." Mikol V., Baumann G., Zurini M.G.M., Hommel U. J. Mol. Biol. 254:86-95(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 482-583.
[48]	"Structure and ligand recognition of the phosphotyrosine binding domain of Shc." Zhou M.-M., Ravichandran K.S., Olejniczak E.F., Petros A.M., Meadows R.P., Sattler M., Harlan J.E., Wade W.S., Burakoff S.J., Fesik S.W. Nature 378:584-592(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 127-317.
[49]	"Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor." Zhou M.-M., Meadows R.P., Logan T.M., Yoon H.S., Wade W.S., Ravichandran K.S., Burakoff S.J., Fesik S.W. Proc. Natl. Acad. Sci. U.S.A. 92:7784-7788(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 480-583 IN COMPLEX WITH TYROSINE-PHOSPHORYLATED CD3Z.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X68148 mRNA. Translation: CAA48251.1.
U73377 mRNA. Translation: AAB49972.1.
Y09847 Genomic DNA. Translation: CAA70977.1.
AK292143 mRNA. Translation: BAF84832.1.
AK315842 mRNA. Translation: BAF98733.1.
AB451255 mRNA. Translation: BAG70069.1.
AB451379 mRNA. Translation: BAG70193.1.
AL451085 Genomic DNA. Translation: CAI13248.1.
AL451085 Genomic DNA. Translation: CAI13249.1.
AL451085 Genomic DNA. Translation: CAI13250.1.
AL451085 Genomic DNA. Translation: CAI13251.1.
AL451085 Genomic DNA. Translation: CAI13254.1. Sequence problems.
CH471121 Genomic DNA. Translation: EAW53168.1.
CH471121 Genomic DNA. Translation: EAW53169.1.
CH471121 Genomic DNA. Translation: EAW53170.1.
CH471121 Genomic DNA. Translation: EAW53171.1.
BC014158 mRNA. Translation: AAH14158.1.
BC033925 mRNA. Translation: AAH33925.1.

IPI

IPI00021326.
IPI00643176.
IPI00643863.
IPI00943132.
IPI00973146.
IPI01014876.

PIR

S25776.

RefSeq

NP_001123512.1. NM_001130040.1.
NP_001123513.1. NM_001130041.1.
NP_001189788.1. NM_001202859.1.
NP_003020.2. NM_003029.4.
NP_892113.4. NM_183001.4.

UniGene

Hs.433795.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MIL	X-ray	2.70	A	482-583	[»]
1N3H	NMR	-	A	111-317	[»]
1OY2	NMR	-	A	111-317	[»]
1QG1	NMR	-	I	423-435	[»]
1SHC	NMR	-	A	127-317	[»]
1TCE	NMR	-	A	480-583	[»]
1WCP	model	-	A	127-583	[»]
2L1C	NMR	-	A	127-317	[»]

DisProt

DP00154.

ProteinModelPortal

P29353.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-699N.

IntAct

P29353. 36 interactions.

MINT

MINT-123530.

PTM databases

PhosphoSite

P29353.

Polymorphism databases

DMDM

182676455.

Proteomic databases

PaxDb

P29353.

PRIDE

P29353.

Protocols and materials databases

DNASU

6464.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368445; ENSP00000357430; ENSG00000160691.
ENST00000368449; ENSP00000357434; ENSG00000160691.
ENST00000368450; ENSP00000357435; ENSG00000160691.
ENST00000368453; ENSP00000357438; ENSG00000160691.
ENST00000448116; ENSP00000401303; ENSG00000160691.

GeneID

6464.

KEGG

hsa:6464.

UCSC

uc001ffv.3. human.
uc001ffw.3. human.
uc001ffx.3. human.

Organism-specific databases

CTD

6464.

GeneCards

GC01M154934.

HGNC

HGNC:10840. SHC1.

HPA

CAB005374.
CAB016305.
HPA001844.

MIM

600560. gene.

neXtProt

NX_P29353.

PharmGKB

PA35746.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG315087.

HOVERGEN

HBG050121.

KO

K06279.

OMA

NPAVNGS.

PhylomeDB

P29353.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
bcr_5pathway. BCR signaling pathway.
endothelinpathway. Endothelins.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
epopathway. EPO signaling pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
fgf_pathway. FGF signaling pathway.
igf1_pathway. IGF1 pathway.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
il4_2pathway. IL4-mediated signaling events.
insulin_pathway. Insulin Pathway.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
pdgfrapathway. PDGFR-alpha signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ptp1bpathway. Signaling events mediated by PTP1B.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
tgfbrpathway. TGF-beta receptor signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P29353.

Gene expression databases

ArrayExpress

P29353.

Bgee

P29353.

Genevestigator

P29353.

GermOnline

ENSG00000160691. Homo sapiens.

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

BindingDB

P29353.

ChEMBL

CHEMBL5626.

ChiTaRS

SHC1. human.

EvolutionaryTrace

P29353.

GenomeRNAi

6464.

NextBio

25115.

SOURCE

Search...

Entry information

Entry name

SHC1_HUMAN

Accession

Primary (citable) accession number: P29353
Secondary accession number(s): B5BU19 , D3DV78, O15290, Q5T180, Q5T183, Q5T184, Q5T185, Q5T186, Q8N4K5, Q96CL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	April 8, 2008
Last modified:	May 29, 2013
This is version 162 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.