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SHC-transforming protein homolog 1 (Src homology 2 domain adapter homolog 1)

 SHCH1_CAEEL             Reviewed;         316 AA.
Q9TYT3; H2KZG0; H2KZG2;
22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
08-MAY-2019, entry version 138.
RecName: Full=SHC-transforming protein homolog 1 {ECO:0000250|UniProtKB:P29353};
AltName: Full=Src homology 2 domain adapter homolog 1 {ECO:0000305};
Name=shc-1 {ECO:0000312|WormBase:F54A5.3a};
ORFNames=F54A5.3 {ECO:0000312|WormBase:F54A5.3a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, INTERACTION WITH DAF-2 AND MEK-1, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=18832074; DOI=10.1101/gad.478408;
Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R.,
Hertweck M.;
"SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to
modulate life span and stress response in C. elegans.";
Genes Dev. 22:2721-2735(2008).
[3] {ECO:0000305}
FUNCTION, INTERACTION WITH MEK-1 AND MLK-1, TISSUE SPECIFICITY, AND
MUTAGENESIS OF ARG-136 AND ARG-234.
PubMed=18809575; DOI=10.1128/MCB.00938-08;
Mizuno T., Fujiki K., Sasakawa A., Hisamoto N., Matsumoto K.;
"Role of the Caenorhabditis elegans Shc adaptor protein in the c-Jun
N-terminal kinase signaling pathway.";
Mol. Cell. Biol. 28:7041-7049(2008).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MLK-1.
PubMed=23072806; DOI=10.1038/ncomms2136;
Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
Hisamoto N.;
"Endocannabinoid-Goalpha signalling inhibits axon regeneration in
Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
Nat. Commun. 3:1136-1136(2012).
[5]
FUNCTION, INTERACTION WITH SVH-2 AND SVH-4, AND MUTAGENESIS OF
ARG-234.
PubMed=27984580; DOI=10.1371/journal.pgen.1006475;
Hisamoto N., Nagamori Y., Shimizu T., Pastuhov S.I., Matsumoto K.;
"The C. elegans discoidin domain receptor DDR-2 modulates the Met-like
RTK-JNK signaling pathway in axon regeneration.";
PLoS Genet. 12:E1006475-E1006475(2016).
-!- FUNCTION: Scaffold protein which plays an important role in the
activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1;
by bringing together mek-1 and mlk-1, promotes mlk-1-mediated
phosphorylation and activation of mek-1 which in turn
phosphorylates kgb-1 (PubMed:18832074, PubMed:18809575). In
addition, negatively modulates the activation of the insulin/IGF-
1-like signaling (IIS) probably by inhibiting the insulin receptor
daf-2. Positively regulates the activity of the transcription
factor daf-16/FOXO by both inhibiting IIS and activating the JNK
pathway (PubMed:18832074). Involved in the response to several
environmental stresses including heavy metal ions (Cu(2+) and
Cd(2+)), heat, oxidative and protein misfolding (ER) stresses
(PubMed:18832074, PubMed:18809575). Plays a role in life span and
egg laying (PubMed:18832074, PubMed:23072806). Plays a role in
axon regeneration after injury (PubMed:23072806, PubMed:27984580).
{ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:23072806, ECO:0000269|PubMed:27984580}.
-!- SUBUNIT: Interacts (via PID domain) with daf-2 (via cytoplasmic
domain) (PubMed:18832074). Interacts with mek-1; the interaction
is independent of mek-1 catalytic activity and is constitutive
(PubMed:18832074, PubMed:18809575). Interacts (via N-terminus)
with mlk-1 (via NPQY motif when phosphorylated on tyrosine
residue) (PubMed:18809575, PubMed:23072806). Does not interact
with jkk-1 or sek-1 (PubMed:18809575). Interacts (via SH2 domain)
with svh-2 (PubMed:27984580). Interacts with svh-4
(PubMed:27984580). {ECO:0000269|PubMed:18809575,
ECO:0000269|PubMed:18832074, ECO:0000269|PubMed:23072806,
ECO:0000269|PubMed:27984580}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832074}.
Nucleus {ECO:0000269|PubMed:18832074}. Cell membrane
{ECO:0000269|PubMed:18832074}; Peripheral membrane protein
{ECO:0000269|PubMed:18832074}. Note=In intestinal cells, enriched
in the nucleus. {ECO:0000269|PubMed:18832074}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:F54A5.3a};
IsoId=Q9TYT3-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:F54A5.3b};
IsoId=Q9TYT3-2; Sequence=VSP_057798, VSP_057801;
Note=No experimental confirmation available. {ECO:0000305};
Name=d {ECO:0000312|WormBase:F54A5.3d};
IsoId=Q9TYT3-3; Sequence=VSP_057799, VSP_057800;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in hypodermis, intestine, head and
tail neurons, pharynx, gonads, vulva and body muscles.
{ECO:0000269|PubMed:18809575, ECO:0000269|PubMed:18832074}.
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EMBL; BX284601; CCD68061.1; -; Genomic_DNA.
EMBL; BX284601; CCD68062.1; -; Genomic_DNA.
EMBL; BX284601; CCD68064.1; -; Genomic_DNA.
PIR; T33836; T33836.
RefSeq; NP_490799.2; NM_058398.4. [Q9TYT3-1]
RefSeq; NP_490800.2; NM_058399.4.
SMR; Q9TYT3; -.
DIP; DIP-25661N; -.
IntAct; Q9TYT3; 2.
STRING; 6239.F54A5.3a; -.
EPD; Q9TYT3; -.
PaxDb; Q9TYT3; -.
PeptideAtlas; Q9TYT3; -.
EnsemblMetazoa; F54A5.3a; F54A5.3a; WBGene00018788. [Q9TYT3-1]
GeneID; 3565745; -.
KEGG; cel:CELE_F54A5.3; -.
UCSC; F54A5.3a; c. elegans. [Q9TYT3-1]
CTD; 3565745; -.
WormBase; F54A5.3a; CE30804; WBGene00018788; shc-1.
WormBase; F54A5.3b; CE20862; WBGene00018788; shc-1.
WormBase; F54A5.3d; CE29391; WBGene00018788; shc-1.
eggNOG; KOG3697; Eukaryota.
eggNOG; ENOG410XTJN; LUCA.
GeneTree; ENSGT00950000182870; -.
HOGENOM; HOG000017678; -.
InParanoid; Q9TYT3; -.
KO; K06279; -.
OMA; CHQLGIC; -.
OrthoDB; 1351843at2759; -.
PhylomeDB; Q9TYT3; -.
SignaLink; Q9TYT3; -.
PRO; PR:Q9TYT3; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00018788; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:WormBase.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:WormBase.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:WormBase.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:WormBase.
GO; GO:0010038; P:response to metal ion; IMP:WormBase.
CDD; cd09925; SH2_SHC; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035676; SHC_SH2.
Pfam; PF00640; PID; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00462; PTB; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS01179; PID; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Nucleus; Reference proteome; SH2 domain; Stress response.
CHAIN 1 316 SHC-transforming protein homolog 1.
{ECO:0000305}.
/FTId=PRO_0000433512.
DOMAIN 16 158 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 211 307 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
SITE 234 234 Required for interaction with svh-2.
{ECO:0000269|PubMed:27984580}.
VAR_SEQ 71 81 VIGEVKKENFP -> PTLHGSMKKPR (in isoform
b). {ECO:0000305}.
/FTId=VSP_057798.
VAR_SEQ 72 76 IGEVK -> DQKSR (in isoform d).
{ECO:0000305}.
/FTId=VSP_057799.
VAR_SEQ 77 316 Missing (in isoform d). {ECO:0000305}.
/FTId=VSP_057800.
VAR_SEQ 82 316 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_057801.
MUTAGEN 136 136 R->K: Partial sensitivity to Cu(2+). May
prevent interaction with mlk-1 when
phosphorylated at Tyr-209 which in turn
may prevent the interaction between mlk-1
and mek-1. No effect on the association
with mek-1. Severe sensitivity to Cu(2+)
and no effect on the association with
mek-1; when associated with K-234.
{ECO:0000269|PubMed:18809575}.
MUTAGEN 234 234 R->K: Weak sensitivity to Cu(2+). Severe
sensitivity to Cu(2+) and no effect on
the association with mek-1; when
associated with K-136. Abolishes
interaction with svh-2.
{ECO:0000269|PubMed:18809575,
ECO:0000269|PubMed:27984580}.
SEQUENCE 316 AA; 35170 MW; D370FF4B941F97E1 CRC64;
MLNVEPSFAE ELRSSGVSLS ATYLGSVPVV ESINVMVSEM RVQVVSECIQ HVAATVGVTA
AREINPVVSR VIGEVKKENF PVDINISSKM IKIIKQSRLI QRHPFSFFSF GAQGQKGTDT
ELMFGYIAKN KDGTDRRCHV VFIEDVHKLI DVLTTAINVN TFDAQANAST SNDGFTVPAP
PMRHRSSLHR QSFVSNCRAP TVTEDVVGKV WYHGNLSRED AQALLKTEGD FLVRQSDHTP
GKYVLSGRTA ENEHKHLILL DNHNRVRTRD RTFSNISELI DYHVNNGMAV RSEGRDRETS
LNLIRPVPCP GSDDIE


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Related Genes :
[shc-1 F54A5.3] SHC-transforming protein homolog 1 (Src homology 2 domain adapter homolog 1)
[SHC1 SHC SHCA] SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Shc1 Shc ShcA] SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Shc1] SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[SHC3 NSHC SHCC] SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (Protein Rai) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
[SRC SRC1] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Shc3 Nshc ShcC] SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
[TSC22D1 KIAA1994 TGFB1I4 TSC22 hucep-2] TSC22 domain family protein 1 (Cerebral protein 2) (Regulatory protein TSC-22) (TGFB-stimulated clone 22 homolog) (Transforming growth factor beta-1-induced transcript 4 protein)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[FERMT2 KIND2 MIG2 PLEKHC1] Fermitin family homolog 2 (Kindlin-2) (Mitogen-inducible gene 2 protein) (MIG-2) (Pleckstrin homology domain-containing family C member 1) (PH domain-containing family C member 1)
[SHC1] SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Fermt2 Plekhc1] Fermitin family homolog 2 (Kindlin-2) (Pleckstrin homology domain-containing family C member 1)
[BLNK BASH SLP65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[SOS1] Son of sevenless homolog 1 (SOS-1)
[rush EG:80H7.5 CG14782] Pleckstrin homology domain-containing family F member 1 homolog (PH domain-containing family F member 1 homolog) (Protein rush hour)
[Blnk Bash Ly57 Slp65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[Notch1 Motch] Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[SUMO1 SMT3C SMT3H3 UBL1 OK/SW-cl.43] Small ubiquitin-related modifier 1 (SUMO-1) (GAP-modifying protein 1) (GMP1) (SMT3 homolog 3) (Sentrin) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (Ubiquitin-like protein UBL1)
[PLEKHM1 KIAA0356] Pleckstrin homology domain-containing family M member 1 (PH domain-containing family M member 1) (162 kDa adapter protein) (AP162)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[App] Amyloid-beta A4 protein (ABPP) (APP) (Alzheimer disease amyloid A4 protein homolog) (Amyloid precursor protein) (Amyloid-beta precursor protein) (Amyloidogenic glycoprotein) (AG) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (APP-C99) (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (APP-C59) (Amyloid intracellular domain 59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (APP-C57) (Amyloid intracellular domain 57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AID(50)) (Gamma-CTF(50)); C31]
[SRC] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[nth-1 R10E4.5] Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[NAV2 HELAD1 KIAA1419 POMFIL2 RAINB1 STEERIN2] Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)
[Sav1 Ww45 Wwp3] Protein salvador homolog 1 (45 kDa WW domain protein) (mWW45)
[THOC5 C22orf19 KIAA0983] THO complex subunit 5 homolog (Functional spliceosome-associated protein 79) (fSAP79) (NF2/meningioma region protein pK1.3) (Placental protein 39.2) (PP39.2) (hTREX90)

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